curriculum of m.sc. biochemistry from academic year 2017 ... · department of biochemistry dst-fist...
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Curriculum of M.Sc. Biochemistry
From Academic Year 2017-2018 Onwards
Department of Biochemistry
Bharathidasan University- Trichy
Programme Outcomes
• PG Granduands are Professionally Competent with characteristic Knowledge-bank, Skill-
set, Mind-set and Pragmatic Wisdom in their chosen fields.
• PG Granduands demonstrate the desired sense of being Seasoned and exhibit unequivocal
Spiritedness with excellent qualities of productive contribution to society and nation in the
arena Science and Technology.
• PG Graduands are mentored such that they exert Leadership Latitude in their chosen fields
with commitment to novelty and distinction.
• PG Graduants are directed in understanding of ethical principles and responsibilities, moral
and social values in day-to-day life thereby attaining Cultural and Civilized personality.
• PG Graduants of are able to Collate information from different kinds of sources and gain a
coherent understanding of the subject.
PROGRAM SPECIFIC OUTCOME
1. The course aims in gaining an understanding of the processes of metabolic
transformation at the molecular level and how these processes are studied.
2. It is important to study enzymes, the rate limiting molecule of all the chemical
reactions and understanding enzymes could pave research ideas.
3. Students can make the Knowledge of the relationship between structure and function
at organ and/or organism level, of important cell biological communication
principles and processes, and how they are regulated.
4. Students can able to Characterize certain functionalities of biomolecules by using
spectroscopic technique
5. Students will gain conceptual understanding of subject matter, scientific reasoning
skills, laboratory manipulative skills.
6. The course aims to give participants a basic knowledge of mechanisms of signal
transduction and the significance of signal transduction in physiology and
pathophysiology.
7. Students can understand the capacity to evaluate and synthesise information from a
wide range of sources in order to communicate ideas, concepts and construct
arguments in both non-scientific and scientific language.
8. Students will learn at the end of the course to conserve the nature and will be able to
develop new strategies to preserve the sources of life.
DEPARTMENT OF BIOCHEMISTRY
DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES
BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI 620 024
M.Sc. DEGREE PROGRAMME IN BIOCHEMISTRY (SEMESTER PATTERN-AUTONOMOUS)
CHOICE BASED CREDIT SYSTEM – (CBCS) (For the candidates admitted from the academic year 2017-18 onwards)
REGULATIONS
1. Name of the Programme
Bharathidasan University is offering a two-year M.Sc. Degree Programme in
Biochemistry to be conducted in the Department of Biochemistry, School of Life
Sciences, Bharathidasan University.
2. Eligibility for admission to the Programme
A candidate who has passed B.Sc. Degree Examination of Bharathidasan
University with Biochemistry/ Chemistry / Zoology /Botany / Nutrition &
Dietetics / Food Science/ Microbiology / Biotechnology as the Major subject or
an examination of any other University accepted by the Syndicate of
Bharathidasan University as equivalent to the B.Sc. degree examination of
Bharathidasan University may be permitted to qualify for the M.Sc. Degree in
Biochemistry by undergoing courses and appear for the examinations of this
Department. A candidate for admission to the programme shall not be more
than 25 years of age as on 1st July of the year of admission.
3. Duration of the Programme
The Programme is for a period of two years. Each year shall consist of two
semesters namely Odd and Even semesters. Odd semesters shall commence
from July and even semesters from December. There shall not be less than 90
working days which shall comprise 450 teaching hours for each semester
(exclusive of the days for the conduct of University end-semester examinations).
4. Scheme of the Examination
I. There shall be examinations at the end of each semester, for odd semesters in the month of October / November; for even semesters in April / May.
II. A candidate who does not pass the examination in any course(s) may be permitted to appear in such failed course (s) in the subsequent examinations to be held in October / November or April / May. However candidates who have arrears in Practicals shall be permitted to take their arrear Practical examination only along with Regular Practical examination in the respective semester.
III. A candidate should get registered for the first semester examination. If registration is not possible owing to shortage of attendance beyond condonation limit / regulation prescribed OR belated joining OR on medical grounds, the candidates are permitted to move to the next semester. Such candidates shall re-do the missed semester after completion of the course.
IV. Viva-Voce: Each candidate shall be required to appear for Viva-Voce Examination (in defence of the Project only).
V. For the Project Report, the maximum marks will be 75 per cent and for the Viva-Voce it is 25 per cent.
VI. A candidate who could not earn credits in certain course(s) of the first,
second and third semesters will be permitted to appear in such course(s)
along with the courses in any subsequent semester examination.
Semester Courses
I
4 Core Courses
1 Laboratory Course
II
2 Core Courses
1 Elective Course
1 ED Course
1 Laboratory Course
III
2 Core Courses
1 Elective Course
1 ED Course
1 Laboratory Course
IV
1 Project
* ED : Extra Disciplinary
➢ The Core Courses (CC), Laboratory courses (LC) and Elective Courses
(EC) will be offered by the Department of Biochemistry and ED course
(EDC) shall be offered by the various Departments of the University
➢ The failed candidates in one EC / EDC are permitted to opt for another EC /
EDC Or they are permitted to continue with the same EC / EDC.
➢ The maximum marks for the examination conducted for each course
is 100, out of which 75 is for University Examination (UE) and 25 is
for Continuous Internal Assessment (CIA).
➢ Grade “AAA” means absent for the UE for the course.
➢ The number of contact hours per week for any course shall range
from three to six hours.
➢ The examinations will be conducted by the Department.
➢ Duration for UE for theory shall be three hours and for practical three
to six hours.
➢ To qualify for the degree, the candidate has to earn at least 72 credits
by way of earning at least 44 credits in Core courses, at least 6 credits
in the Elective courses, 4 credits in ED courses and 18 credits in the
Project Work mentioned above.
➢ The content of the syllabus for each course is divided into six units
and the sixth unit is been excluded for examination. However, the
topic will be discussed on the regular class hours.
➢ In the case of courses with practical component, 75 is for University
Practical Examination (UE) and 25 is for Continuous Internal
Assessment (CIA).
➢ The syllabi will be framed by the Board of Studies consisting of all the
members of the faculty in the Department and experts from outside
the department (approved by the University) with Head of the
Department as the Chairperson.
➢ There is no provision for improvement of marks in UE and CIA in any
course.
➢ In the statement of marks, both the mark obtained by the candidate
and the grade awarded to him/her will be mentioned.
➢ The whole programme must be completed within 4(four) years from
the date of joining; otherwise the registration for the programme will
be cancelled.
5. Project
Each candidate shall be required to take up a Project Work; submit Project
Report at the end of the second year. The Head of the Department shall assign
the Guide who in turn will suggest the Project Work to the student in the
beginning of fourth semester. Two typed copies of the Project Report shall be
submitted to the Department on or before the date fixed by the Department
Head.
The Dissertation will be evaluated by Examiners, nominated by the Department.
The candidate concerned will have to defend his project in a Viva-Voce
examination
6. Credits
The term “Credit‟ refers to the weightage given to a course, usually in relation to
the instructional hours assigned to it. For instance, a six hour course is assigned
four credits, four/ five hour course is assigned three credits and two hour
course is given two credits. However, in no instance the credits of a course can
be greater than the hours allotted to it.
The total minimum credits, required for completing a PG programme is 72. The
details of credits for individual components and individual courses are given in
Table.
7. Attendance
➢ Every student should put in at least 75% attendance in each course.
➢ In each semester every candidate must compulsorily register for the
examination in all the courses attended in that semester.
➢ No candidate who has put in attendance for less than 75% of the
working days in a semester will be permitted to take the UE pertaining
to that semester unless he/she gets condonation certificate.
➢ On the day, on which a course is concluded, the Course Teacher of the
course shall intimate the Head of the Department the particulars of all
students who have shortage of attendance in the course offered by
him/her.
➢ A candidate who has put in less than 65% attendance in a course,
he/she has to either repeat the course or take an equivalent course.
➢ Condonation of shortage of attendance shall be given as per the
provisions given below:
o Students must have 75% of attendance in each course for appearing
the examination. Students who have 74% to 70% of attendance shall
apply for condonation in the prescribed form with the prescribed fee
of Rs.500/- (Rupees Five hundred only). Students who have 69% to
65% of attendance shall apply for condonation in prescribed form
with the prescribed fee of Rs.500/- (Rupees Five hundred only) along
with the Medical Certificate.
o Students who have below 65% of attendance are not eligible to
appear for the examination. They shall re-do the semester(s) after
completion of the programme.
o The Head of the Department shall announce the names of all students
who will not be eligible to take the end-semester examination in the
various courses due to shortage of attendance.
8. Question Paper Pattern Part A
Ten Questions ( No choice) 10 x 2 = 20 marks Two Questions from each Unit
Part B Five Questions (either or type) 5 x 5 = 25 marks
One Question from each Unit Part C
Three Questions out of five 3 x 10 = 30 marks One Question from each unit
9. Evaluation
The performance of a student in each course is evaluated in terms of
percentage of marks with a provision for conversion to grade points.
Evaluation for each course shall be done by a continuous internal
assessment by the concerned Course Teacher as well as by an end
semester examination and will be consolidated at the end of the course.
The components for continuous internal assessment are :
Two tests - 15 Marks (Third / repeat tests for genuine absentees)
Seminar - 5 Marks
Assignments - 5 Marks
--------------
Total: 25 Marks
--------------
Attendance need not be taken as a component for continuous
assessment, although the students should put in a minimum of 75%
attendance in each course. In addition to continuous evaluation
component, the end semester examination, which will be a written-
examination of at least 3 hours duration, would also form an integral
component of the evaluation. The ratio of marks to be allotted to
continuous internal assessment and to end semester examination is 25 :
75. The evaluation of laboratory component, wherever applicable, will
also be based on continuous internal assessment and on an end-semester
practical examination.
10. Passing Minimum
➢ A candidate shall be declared to have passed in each course if he/she
secures not less than 40% marks in the University Examinations and
40% marks in the Internal Assessment and not less than 50% in the
aggregate, taking Continuous assessment and University Examinations
marks together.
➢ Failed candidates in the Internal Assessment are permitted to improve
their Internal Assessment marks in the subsequent semesters (2
chances will be given) by writing the CIA tests and by submitting
assignments.
➢ Candidates, who have secured the pass marks in the end-semester
Examination (U.E.) and in the C.I.A. but failed to secure the aggregate
minimum pass mark (E.S.E. + I.A.) are permitted to improve their
Internal Assessment mark in the following semester and / or in
University Examinations.
➢ A candidate shall be declared to have passed in the Project work if
he/she gets not less than 40% in each of the Project Report and
Viva/Voce but not less than 50% in the aggregate of both the marks for
Project Report and Viva-Voce.
➢ A candidate who gets less than 40% in the Project Report must
resubmit the Project report.
➢ Such candidates need to take the Viva-Voce on the resubmitted Project.
11. Letter Grade and Grade Points of the Courses and Final Result
Once the marks of the CIA and end-semester examinations for each of the
course are available, they will be added. The marks, thus obtained will
then be graded as per the scheme provided in the following Table.
Grade Point Letter Grade
96 and above 10 S+
91-95 9.5 S
86-90 9.0 D++
81-85 8.5 D+
76-80 8.0 D
71-75 7.5 A++
66-70 7.0 A+
61-65 6.5 A
56-60 6.0 B
50-55 5.5 C
Below 50 0 F
From the second semester onwards the total performance within a
semester and continuous performance starting from the first semester are
indicated respectively by Grade Point Average (GPA) and Cumulative
Grade Point Average (CGPA). These two are calculated by the following
formulae:
n
∑CiGi
i = 1
GPA = ------------------------
n
∑Ci
i = 1
Where ‘Ci’ is the Credit earned for the Course i in any semester; ‘Gi’ is the
Grade Point obtained by the student for the Course i and ‘n’ is the number
of Courses passed in that semester. CGPA = Average Grade Points of all the
Courses passed starting from the first semester to the current semester.
Final Result
* Absence from an examination shall not be taken as an attempt.
12. Instant Examination
The department will conduct instant examination to a candidate in May/June if
only one course remains to be cleared by him/her to qualify for the degree.
13. Revision of Regulations and Curriculum
The Department from time to time revise, amend and change the regulations
and the curriculum, if found necessary.
CGPA Letter Grade Classification of Final Result
9.51 and
above
S+
First Class - Exemplary
9.01-9.50 S
8.51-9.00 D++
First Class – Distinction 8.01-8.50 D+
7.51-7.50 D
6.51-7.00 A++
First Class 6.01-6.50 A+
5.51-6.00 A
5.00-5.50 B Second Class
5.00-5.50 C
Below 5.00 F Fail
DEPARTMENT OF BIOCHEMISTRY
SCHOOL OF LIFE SCIENCES
BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI 620 024
M.Sc. DEGREE PROGRAMME IN BIOCHEMISTRY (CBCS)
(For the candidates to be admitted from the year 2017-18 onwards)
Semester Courses
I
4 Core Courses
1 Laboratory Course
II
2 Core Courses
1 Elective Course
1 ED Course
1 Laboratory Course
III
2 Core Courses
1 Elective Course
1 ED Course
1 Laboratory Course
IV
1 Project
DEPARTMENT OF BIOCHEMISTRY, BHARATHIDASAN UNIVERSITY,
TIRUCHIRAPPALLI-24
M.Sc. Biochemistry Course Structure (2017 – 2018 onwards)
SEM Category Code Courses Hrs Crs
I
Core 1 BC101 Biomolecules 6 6
Core 2 BC102 Enzymes 6 6
Core 3 BC103 Cell and Molecular Biology 6 6
Core 4 BC104 Biochemical Techniques 6 6
Core 5 BC105 Laboratory Courses-I 6 4
Total for Semester-I 30 28
II
Core 6 BC 201 Biochemistry of Signal Transduction & Regulation 6 6
Core 7 BC 202 Intermediary Metabolism 6 6
Elective BC 203 Elective- I 5 3
Core 8 BC 204 Laboratory Courses –II 6 4
Non major
Elective
BC2ED ED-I 3 2
Total for Semester II 26 21
III
Core 9 BC 301 Immunology 6 6
Core 10 BC 302 Genetic Engineering and Molecular Techniques 6 6
Elective BC 303 Elective - II 5 3
Core 11 BC 304 Laboratory Courses -III 6 4
Non major
Elective
BC3ED ED-II 3 2
Total for Semester III 26 21
IV
BC 401 Project & Viva Voice 30 20
Total for Semester IV 30 20
Total hours & credits 112 90
Elective
BC203 Ecology and Environmental Biology
BC205 Bioinformatics
BC206 Biostatistics
BC207 Chromatin and Epigenetics
BC303 Clinical Biochemistry
BC305 Membrane Biochemistry
BC306 Concept in Neurochemistry
Non Major Elective
BC3ED Developmental Biology
BC2ED Genetics
BC3ED-I Computational Biology
BC101 - BIOMOLECULES
(Core 1)
SEM: I Lecture/Week: 6
BC101 Credits: 6
Objectives
i. To list out the structure and functions of biological macromolecules.
ii. To learn the metabolism and integration of biomolecules that takes place in human
system.
iii. Integrate the various aspects of metabolism and their regulatory pathways
iv. Students can understand the fundamental energetics of biochemical processes
v. To elaborate the relation between biochemical defects and metabolic disorders.
vi. To enumerate the organization of signalling pathways.
UNIT- I
HOMO AND HETEROGLYCANS: Polysaccharides - occurrence, structure, properties
and functions of homoglycans - starch, glycogen, cellulose, dextrin, inulin, chitin, xylans
and galactans. Occurrence, structure, properties and functions of heteroglycans - hyaluronic
acid, keratan sulphate and chondroitin sulphate. Bacterial cell wall polysaccharides, Blood
group substances, Sialic acid. Glycoproteins and their biological functions. Lectins structure
and functions. ( https://biologydictionary.net/polysaccharide)
Unit - II
PROTEINS: Classification, structure and properties of amino acids, Essential and non-
essential amino acids. Non protein amino acids. Proteins - Classification based on solubility,
shape, composition and function. Properties of proteins. Denaturation and renaturatton of
proteins. Structure of peptide bonds. Chemical synthesis of polypeptides. Protein structure -
Primary, secondary, tertiary and quaternary structures of protein. Forces stabilizing the
secondary, tertiary and quaternary structures of proteins. Structure and biological functions
of fibrous proteins (keratins, collagen and elastin), globular proteins (hemoglobin,
myoglobin), lipoproteins, metalloproteins, glycoprotein and nucleoproteins.(chalk and talk)
Unit - III
LIPIDS: Definition and classification of lipids. Fatty acids - classification, nomenclature,
structure and properties. Triacylglycerols. Classification, structure and function of
prostaglandins, thromboxanes and leukotrienes. Chemical properties and functions of
phospholipids and their structures - lecithins, cephalins, phosphatidyl serine, phosphatidyl
inositol, plasmalogens. Glycolipids (cerebrosides and gangliosides), Isoprenoids and sterols
(cholesterol and zymosterol), steroids (steroid hormones), bile acids and bile salts. Types
and functions of plasma lipoproteins. (https://www2.chemistry.msu.edu/faculty/reusch/virttxtjml/lipids.htm)
Unit - IV
NUCLEIC ACIDS: Structure of purines and pyrimidines. Components of nucleic acids -
nucleosides, nucleotides, and poly nucleotides. Occurrence and isolation of nucleic acids.
Properties of DNA: buoyant density,viscosity, hypochromicity, denaturation and
renaturation– the cot curve. Chemical synthesis of oligonucliotides. DNA: structure of
different types (A, B and Z DNA), biological role, polymorphism. Structure and role of
different types of RNA. (Problem based learning*)
UNIT-V
VITAMINS AND PORPHYRINS: Structure and biochemical properties of water soluble
and fat soluble vitamins and their coenzyme activity. Macro minerals (Ca, P, Mg, Na, K, Cl)
and micro minerals/trace elements (Co, I, Fe, Mn, Zn, and F) - their sources, daily
requirements, functions and deficiency diseases symptoms. Porphyrins the porphyrin ring
system, chlorophyll, hemoglobin, myoglobin and cytochrome.
Unit VI:
Advanced studies in various metabolic pathways and significance of macromolecules,
Enzymatic control of metabolic pathways, Metabolic profiles of key tissues, Hormonal
control of pathways.
Recommended Books:
1) L. Stryer. 2002. Biochemistry, 5th edition. W.H.Freeman & Company, New York
2) Horton, R., Moranm, LA., Scrimgeour, G, MarcPerry and David Rawn. 2006.
Principles of Biochemistry, 4th edition.
3) A. L. Lehninger, Nelson & Cox. 2007. Principles of Biochemistry, 5th edition, CBS,
India.
4) Murray R. K. et al. Harpers Illustrated Biochemistry, 2009, 28th edition. Lange
Medical Books/McGraw-Hill.
5) Zubay, 2005. Principles of Biochemistry, 4th edition. Prentice hall.
6) Richard Harvey, Denise Ferrier. 2005. Lippincott. Outlines of Biochemistry, 5th
edition.
COURSE OUTCOME:
i) To understand the structure and functions of biological macromolecules.
ii) To learn the metabolism and integration of biomolecules that takes place in human
system
iii) Integrate the various aspects of metabolism and their regulatory pathways
iv) Students can understand the fundamental energetics of biochemical processes
v) "To understand the relation between biochemical defects and metabolic
disorders."
vi) To understand the organization of signalling pathways.
vii) To understand the role of membrane processes in metabolism
viii) "Overall, gaining an understanding of the processes of metabolic
transformation at the molecular level and how these processes are studied. "
BC 102 – ENZYMES
(Core 2)
SEM: I Lecture/Week: 6
BC102 Credits: 6
Objectives:
i. Students will obtain basic knowledge about the relationship between properties and
structure of the enzymes, their mechanism of action and kinetics of enzymatic
reactions.
ii. The student could able to analyse the structure/function relationships in biocatalysed
reactions
iii. The student would able to describe the priciples and methods of metabolic
engineering of (micro) organisms to produce industrial chemicals.
iv. Students able to research a contemporary application of enzyme technology or
metabolic engineering and present the results in a well-structured oral
presentation.
v. Students can understand to compare and contrast the historical uses of enzyme
technology with current applications in a diverse range of industries.
Unit - I
Introduction of enzymes: definitions (catalytic power, specificity, reactivity, regulation,
transformation of different forms of energy, Holoenzyme, Apoenzyme, coenzymes and
cofactors). Enzyme Nomenclature and IUB system of enzyme classification. Active site-
Fisher and Koshland models. Formation of enzyme substrate complex evidences. Basic
concepts of bioenergetics: The collision theory, activation energy and transition state theory.
Measurement and expression of enzyme activity – enzyme assays, Investigation of sub-
cellular compartmentation of enzymes and marker enzymes. Enzyme units.
(https://www.medicalnewstoday.com/articles/319704.php)
Unit- II
Enzyme kinetics: Pre-Steady state and Steady state kinetics, Rapid reaction kinetics
(Continuous flow and stopped flow techniques). Kinetics of single substrate enzyme
catalyzed reaction - Michaelis-Menten (Briggs- Haldane) equation, Double-Reciprocal Plot,
Lineweaver Burk plot, Eadie-Hofstee and Hanes-Wolf plots. Determination of Vmax, Km,
Kcat, Specificity constant (Kcat/Km) and their significance. Factors influencing enzymatic
activity, Arrhenius plot. Kinetics of enzyme reactions having two or more substrates. Single
displacement and double displacement reactions.(chalk and talk)
Unit - III
Enzyme inhibition: Reversible and Irreversible inhibition - Competitive, Non-competitive
and mixed inhibition. Substrate inhibition and Feedback inhibition.Determination of
inhibitor constant.Therapeutic, diagnostic and industrial applications of enzyme
inhibitors.Mechanism of enzyme action: Factors contributing to the catalytic efficiency -
proximity and orientation, covalent catalysis, acid-base catalysis, metal ion catalysis, strain
and distortion theory. Mechanism of action of Lysozyme, Carboxy peptidase, Chymotrypsin
and Ribonuclease.( elte.prompt.hu/sites/default/files/tananyagok/.../ch09s04.htm)
Unit IV:
Introduction of co-enzymes: Structure and functions – Pyridine and flavin nucleotides,
coenzyme A, Pyridoxal phosphate and thiamine pyrophosphate, tetrahydrofolate and B12
coenzymes. Allosteric Interactions: Enzyme regulation, allosteric enzymes. Allosteric
kinetics (MWC and KNF models), symmetry and sequential models. Hill’s equation and
Hill’s co-efficient. Enzyme repression and covalent modification of enzymes. Zymogen
activation. Isozymes.
Unit V:
Multienzyme system: Multifunctional enzymes. Multi-enzyme complexes (Pyruvate
dehydrogenase complex, fatty acid synthase and Na - K ATPase), Oligomeric enzymes and
Metalloenzymes. Modern concepts of evolution of catalysts: Catalytic RNA (Ribozymes),
abzymes. Immobilized enzymes and their industrial applications. Chemical modification and
site-directed mutagenesis of enzymes. Industrial applications of enzymes - food and
pharmaceutical enzymes. Biosensors. (blended mode of teaching *)
Unit VI:
Enzyme Structure Activity Relationship (SAR) and Drug Discovery- Properties of
Enzymes: Lead Compound, Structure based drug design, combinatorial chemistry, High-
throughput screening, Case study of DHFR.
Recommended Books:
1. Principles of Biochemistry, 1993. A.L. Lehninger, Nelson & Cox (CBS, India) and
new edition.
2. Biochemistry, 2004, Donald Voet and Judith Voet, John Wiley and sons. ISBN -
047119350
3. Biochemistry, 5th edition, by Lubert Stryer, New York: W H Freeman; 2002, ISBN-
10: 0-7167-3051-0.
4. Text Book of Biochemistry with clinical correlations, 4th edition – Thomas M.
Devlin.
5. Text of Biochemistry, 1908 – West & Todd, MacMillian Publications
6. Principles of Biochemistry, by G. L. Zubay, 1995, Wm. C. Brown
7. Biochemistry 2nd edition Christopher K.Mathews and K.E.VanHoldge (1995)
(Benjamin and cumming).
8. Enzymes. Dixon and Webb 3rd ed. Longmans, 1979.
9. Enzymes in Food Technology. CRC Press, 2001. Whitehurst RJ.
10. Industrial Enzymes and their applications. Uhlig H. John Wiley, 1998.
COURSE OUTCOME:
i) Students will obtain basic knowledge about the relationship between properties and
structure of the enzymes, their mechanism of action and kinetics of enzymatic
reactions.
ii) The student could able to analyse the structure/function relationships in biocatalysed
reactions
iii) The student would able to describe the priciples and methods of metabolic engineering
of (micro)organisms to produce industrial chemicals.
iv) Students able to research a contemporary application of enzyme technology or
metabolic engineering and present the results in a well-structured oral presentation.
v) Students can understand to compare and contrast the historical uses of enzyme
technology with current applications in a diverse range of industries.
vi) At the end of the course students will be explored to understand the use of enzymes in
medicine, food, organic synthesis, genetics and other areas sectors that favor a wide
reach for them.
vii) To integrate the practical aspects of enzymology with the kinetic theories to provide a
mechanistic overview of enzyme activity and regulation in cells
viii) It is important to study ezymes,the rate limiting molecule of all the chemical reactions
and understanding enzymes could pave research ideas.
BC103-CELL AND MOLECULAR BIOLOGY
(Core 3)
SEM: I Lecture/Week: 6
BC103 Credits: 6
Objectives:
i. To have a basic understanding about the morphology of cell & cell organelles and its
function in detail.
ii. To learn the structure, function and molecular mechanism of the genetic material.
iii. Students could able to describe the general principles of gene organization and
expression in both prokaryotic and eukaryotic organisms.
iv. To learn how to interpret the outcome of experiments that involves the use of
recombinant DNA technology and other common gene analysis techniques.
v. To understand how to relate properties of cancerous cells to mutational changes in
gene function.
Unit - I
Cell Introduction: Structure and function prokaryotic and eukaryotic cells. Mechanism of
cell division – mitosis and meiosis, Structure and organization of chromatin. Structure and
function of cell membranes and organelles – mitochondria, chloroplasts (and their genetic
organization) endoplasmic reticulum, Golgi apparatus, lysosomes, peroxisomes and their
functions. Membrane models, lipid assembly and membrane receptors. Intracellular
compartments, secretory and endocytic pathways in protein sorting, cytoskeleton, nucleus,
Membrane transport – active and passive transport. Microtubules and microfilaments. (https://www.diffen.com/difference/Eukaryotic_Cell_vs_Prokaryotic_Cell)
Unit - II
DNA Replication, Repair and Mutation: DNA in prokaryotes and eukaryotes. Mode of
replication; experimental findings of Meselson & Stahl. Enzymes involved in replication,
events on the replication fork and termination, mechanism of replication. Inhibitors of DNA
replication and DNA repair mechanisms (Direct repair, excision repair, mismatch repair,
recombination repair, SOS response, Eukaryotic repair system).Type of damages and
mutation – point mutation and frame shift mutation. Suppressor Gene mutation and
chromosomal aberration.(Blended mode of teaching)
Unit III:
Transcription: Organization of transcriptional unit – prokaryotes and eukaryotes. RNA
polymerases – structure and functions. Promoters, transcription factors, transcription
complex assembly and mechanism of transcription- Operon model. Transcriptional
regulation –hormonal (steroid hormone receptors), phosphorylation (STAT proteins),
activation of transcriptional elongation by HIV tat protein. Post-transcriptional processing.
Alternative splicing. Catalytic RNA (ribozymes), antisense RNA. Inhibitors of transcription.
(https://www.atdbio.com/content/14/Transcription-Translation-and-Replication)
Unit - IV
Translation: The genetic code – specificity, redundancy and wobble hypothesis.
Mitochondrial and chloroplast genetic codons. Components of protein synthesis– mRNA,
rRNA and tRNA. Mechanism of protein synthesis. Regulation of protein synthesis -
constitutive and narrow domain regulation. Inhibition of protein synthesis. Co- and post-
translational modifications. Protein targeting- the signal sequence hypothesis, targeting
proteins to membranes, nucleus and intracellular organelles. Protein degradation - ubiquitin
pathway. Protein folding - models, molecular chaperones.
Unit - V
Gene expression and regulation: Levels of gene expression. Principles of gene regulation.
Upregulation, downregulation, induction and repression. Comparison of gene regulation
strategies in prokaryotes and eukaryotes. Genetic and epigenetic gene regulation by DNA
methylation. Methylation and gene regulation in mammals and plants. Epigenetic gene
regulation by DNA methylation in mammals - role of imprinting and X-chromosome
inactivation.(https://www2.le.ac.uk/projects/vgec/highereducation/topics/geneexpression-
Regulation)
Unit VI:
Cell Migration and its Control Mechanisms, Cell Migration and Neurite Outgrowth,
The Tumour Microenvironment: The Social Environment of the Cancer Cell.
Recommended Books:
1. Molecular Cell Biology, 5th edition, Harvey Lodish, Arnold Berk, Paul Matsudaira, chris
A. Kaiser, Monty Krieger, Mathew P Scott, Lawrence Zipursky, James Darnell, W.H
Freeman & Co. 2004, ISBN - 0716743663
2. Genes VIII, Benjamin Lewin, Pearson Prentice Hall, 2004, ISBN - 0131238264
3. Molecular Biology, David Friefelder, Jones & Bartlett Publishers ISBN 0867200693 (0-
86720-069-3).
4. Molecular Biology of The Cell, 4th edition, Bruce Alberts, Alexander Johnson, Julian
Lewis, Martin Raff, Keith Roberts, and Peter Walter, Garland edition, ISBN-10: 0-8153-
4072-9
5. Cell Biology and Histology, 6th edition, Gartner et al., Lippincott William and Wilkins
Publishers, ISBN - 1608313212.
6. Cell Biology and Molecular Biology, 8th edition, EDP De Robertis and EMF De Robertis,
Lippincott Williams and Wilkins, 2006, ISBN - 0781734932
7. Molecular Biology of the Gene, 6th edition, James D Watson, 2008, Cold Spring Harbor
Laboratory, ISBN 978-080539592-1
8. Becker’s World of The Cell, 8th edition, Jerrf Hardin, Gregory Bertoni, Lewis Kleinsmith,
2011, Pearson Publications, ISBN - 0321709780
9. Cell and Molecular Biology Concepts & Experiments, 5th edition, Gerald Karp, 2008,
wiley Publications, ISBN - 978-0-470-04214-4
COURSE OUTCOME:
i) To have a basic understanding about the morphology of cell & cell organelles and its
function in detail.
ii) To understand the structure, function and molecular mechanism of the genetic
material.
iii) "Students could able to describe the general principles of gene organization and
expression in both prokaryotic and eukaryotic organisms."
iv) To learn how to Interpret the outcome of experiments that involve the use of
recombinant DNA technology and other common gene analysis techniques
v) To understand how to relate properties of cancerous cells to mutational changes in
gene function.
vi) Understand receptor subclasses and their possible uses in cell signalling.
vii) students understand the mechanisms by which different messenger-receptor
interactions bring about long or short-term changes in cell state.
viii) Students can make the Knowledge of the relationship between structure and function
at organ and/or organism level, of important cell biological communication principles
and processes, and how they are regulated.
BC104 - BIOCHEMICAL TECHNIQUES
(Core 4)
SEM: I Lecture/Week: 6
BC104 Credits: 6
Objectives:
i. This course will introduce some of the experimental techniques used in
biochemistry and molecular biology
ii. Students can able to learn methods for purifying proteins, expressing
recombinant proteins in bacterial cells, and analyzing biological molecules by
electrophoresis, Western blotting, and enzyme activity assays.
iii. To be able to communicate and discuss General principles of biochemical
investigation
iv. To perceive the strengths, limitations and creative use of techniques for
problem-solving
v. Familiarity with working principles, tools and techniques of analytical
techniques
Unit - I
Units of measurement of solutes in solution : Normality, Molarity, molality and
milliosmol. Ionic strength.pH, pOH, Henderson – Hesselbalch equation, buffers, pH of body
fluids. Measurement of pH by indicators, Zwitter ions.pH dependent ionization of amino
acids and proteins. Colloids and their application, Viscosity, surface tension and Donnan
membrane equilibrium.Principles of electrochemical techniques – measurement of pH by
glass electrode and hydrogen electrode.Oxygen electrode – principles, operation of a Clarke
electrode and its applications.(Blended mode of teaching)
Unit - II
Cell Fractionation Techniques : Cell lysis, differential and density gradient centrifugation,
Salting in, Salting out, Dialysis, Ultrafiltration. Ultra Centrifugation - preparative and
analytical ultracentrifuge, Svedberg's constant, Sedimentation velocity and Sedimentation
equilibrium, Schleiran optics. Chromatographic Techniques - Principles and Applications of
Paper, TLC, Adsorption, Ion exchanges, Gel filtration, Affinity, GLC, Chromato focusing,
HPLC,FPLC.( https://study.com/academy/lesson/cell-fractionation-definition)-
Unit - III
Electrophoretic Techniques: Polyacrylamide gel electrophoresis, SDS-PAGE, 2D –
PAGE, Isoelectric focusing, Visualizing protein bands – CBB & Silver staining. Agarose
gel Electrophoresis, pulse field electrophoresis, high voltage electrophoresis, Capillary
Electrophoresis, Isotachophoresis, RFLP, FISH. Blotting techniques and its applications –
Western, Northern & Southern.
Unit - IV
Isotopic Tracers: Heavy isotopes and radio isotopes theory. Application of radio isotopes in
Biology - 3H, 14C, 32P, 131I, 35S, concept of half-life, decay constant, detection and
quantitation - GM counter and scintillation counter, solid and liquid scintillation. Quenching
and quench correction, Cerenkov counting. Specific activity, carrier free isotope, isotope
dilution techniques and autoradiography.Radiation hazards and radio dosimetry.
Unit - V
Spectroscopic techniques: colorimetry, spectrophotometry – UV & visible, Principle –
Beer & Lambert’s law, Extinction coefficient. Principle and application - Atomic absorption
spectroscopy, Fluorimetry.Basic principle and application of mass spectra, NMR, ESR, ESI-
MS, MALDI-TOF, CD, MRI, CTscans.Biochips (DNA chips, Protein chips and Sensor
chips).Vibration Spectra – IR and Raman – Principles and Applications.X-ray
crystallography – protein crystals, Bragg’s law.(Blended mode of teaching*)
Unit VI:
Hydrodynamic methods of separation of biomolecules such as viscosity and
sedimentation- their principles, variants and applications. Hydrodynamic voltammetr and its
principle and application.
Recommended Books:
1. Wilson and Walker. A biologists guide to principles and techniques of practical
biochemistry. 5th ed. Cambridge University Press 2000.
2. Boyer, R. Modern Experimental Biochemistry. 3rd ed. Addison Weslery Longman,
2000.
3. Upadhyay, Upadhyay and Nath. Biophysical Chemistry Principles and Techniques.
Himalaya Publ. 1997.
4. Simpson CFA &Whittacker, M. Electrophoretic techniques.
5. Sambrook. Molecular Cloning. Cold Spring Harbor Laboratory, 2001.
6. Friefelder and Friefelder. Physical Biochemistry – Applications to Biochemistry and
Molecular Biology. WH Freeman & Co. 1994.
7. Pavia et al. Introduction to Spectroscopy. 3rd ed. Brooks/Cole Pub Co., 2000.
COURSE OUTCOMES:
i) This course will introduce some of the experimental techniques used in biochemistry
and molecular biology
ii) Students can able to learn methods for purifying proteins, expressing recombinant
proteins in bacterial cells, and analyzing biological molecules by electrophoresis,
Western blotting, and enzyme activity assays.
iii) To be able to communicate and discuss General principles of biochemical
investigation
iv) To understand the strengths, limitations and creative use of techniques for problem-
solving
v) Familiarity with working principles, tools and techniques of analytical techniques
vi) To be able to organize the lab results and write a report on a standard paper format
vii) Students can understand the knowledge for the separation of proteins/peptides by
selecting appropriate separation techniques.
viii) Students can able to Characterize certain functionalities of biomolecules by using
spectroscopic technique
BC105 Lab Course – I
(Core 5)
SEM: I Lecture/Week: 6
BC105 Credits: 4
Objectives
i. Students will develop the habit of being cautious, safe and will learn to follow basic
laboratory rules.
ii. Students will be able to design a experiment and learn to trouble shoot.
iii. The course helps to understand the principles of Instrumentation and promote
working ability
iv. Students will have intense working knowledge on basic scientific equipment and to
analyze the data.
v. Students will have the exposure to perform the experiments individually.
1. Calculation and preparation of standard solution
2. Preparation of buffer, training to use of balance and PH meter
3. Determine pKa and pI of acidic, basic, and neutral amino acid
4. Estimation of amino acids by Ninhydrin methods
5. Estimation of reducing sugar by DNSA method
6. Estimation of protein by Lowry’s method
7. Estimation of DNA by Diphenylamine method
8. Estimation of RNA by Orcinol method
9. Estimation of inorganic phosphorous by Fiske and Subbarow method
10. Determination of calcium in milk by Titration method
11. Separation of purines and pyrimidines by paper chromatography
12. Separation of phospholipids by thin layer chromatography
13. Separation of amino acids by ion exchange chromatography
COURSE OUTCOME:
i) Students will develop the habit of being cautious, safe and will learn to follow basic
laboratory rules.
ii) Students will be able to design a experiment and learn to troubleshoot.
iii) The course helps to understand the principles of Instrumentation and promote working
ability.
iv) Students will have intense working knowledge on basic scientific equipment and to
analyze the data.
v) Students will have the exposure to perform the experiments individually.
vi) Students will know to handle the chemicals practically safe and work based on the
prescribed protocols.
vii) Laboratory studies can create a learning environment that encourages students to
question, thereby fostering critical thinking.
viii) Students will gain conceptual understanding of subject matter, scientific reasoning
skills, laboratory manipulative skills.
BC 201 - BIOCHEMISTRY OF SIGNAL TRANSDUCTION AND REGULATION
(Core 6)
SEM: II Lecture/Week: 6
BC201 Credits: 6
Objectives
i. Helps to distinguish the key principles of biochemical metabolic concepts
ii. Students will learn the signalling pathways that will help them in further studies.
iii. Students grasp the basic need of the signalling molecules and the consequesnce on
their absence.
iv. Students will be exposed to most of the actions of the biological system,which they
will study in depth with signalling molecules.
v. Students can able to understand the function of specific anabolic and catabolic
pathways and how these pathways are controlled and interrelated
Unit - I
Regulation of transcription and translation in prokaryotes: Positive and negative
control, repressor and inducer, concept of operon, lac-, and trp operons, attenuation,
regulons. Regulation in eukaryotes- gene families, regulatory strategies in eukaryotes, gene
alteration, regulation of synthesis of primary transcripts, hormonal control, transcription
factors, transcription factors: targets of signaling pathways, DNA binding motifs in pro- and
eukaryotes, Helix turn, helix, zinc fingers, leucine zippers/ b zip, helix loop helix motifs.
Regulation at the level of translation in prokaryotes and eukaryotes.
(vbio.weebly.com/uploads/.../15.2_-_regulation_of_transcription_and_translation.pptx*)
Unit- II
Signal transduction: definition, signals, ligands and receptors. Endocrine, paracrine and
autocrine signaling. Sensory Transduction : Nerve impulse transmission – Nerve cells,
synapses, reflex arc structure, Resting membrane potential, action potential, voltage gated
ion-channels, impulse transmission, neurotransmitters, neurotransmitter receptors. Rod and
cone cells in the retina, biochemical changes in the visual cycle, photochemical reaction and
regulation of rhodopsin. Odor receptors. Chemistry of muscle contraction – actin and
myosin filaments, theories involved in muscle contraction, mechanism of muscle
contraction, energy sources for muscle contraction.(Chalk and talk*)
Unit - III
Receptors and signaling pathways: cell signaling, cell surface receptors. G Protein coupled
receptors- structure, mechanism of signal transmission, regulatory GTPases, heterotrimeric
G proteins and effector molecules of G Proteins. Receptor tyrosine kinases, Role of
phosphotyrosine in SH2 domain binding. Signal transmission via Ras proteins and MAP
kinase pathways. Signaling molecules- cAMP, cGMP, metabolic pathways for the formation
of inositol triphosphate from phosphatidyl inositol diphosphate, Ca2+, DAG and NO as
signaling molecules, ryanodine and other Ca2+ receptors, phosphoregulation of inositol and
the calcium channel activation. Ser/Thr-specific protein kinases and phosphatases.
Unit - IV
Signaling by nuclear receptors: ligands, structure and functions of nuclear receptors,
nuclear functions for hormones/metabolites - orphan receptors; cytoplasmic functions and
crosstalk with signaling molecules, signaling pathway of the steroid hormone receptors.
Cytokine receptors- structure and activation of cytokine receptors, Jak-Stat path way, Janus
kinases, Stat proteins.
Unit - V
Regulation of the cell cycle: Overview of the cell cycle, cell cycle control mechanisms,
Cyclin-dependent protein kinases (CDKs), regulation of cell cycle by proteolysis, G1/S
Phase transition, G2/M Phase transition, cell cycle control of DNA replication, DNA damage
check points. Cancer, types of cancer, factors causing cancer-physical, chemical and
biological agents. Errors in function of signal proteins and tumerogenesis.Oncogenes, proto-
oncogenes and tumor suppressor genes.Tumor suppressor protein p53 and its role in tumor
suppression.Tumor suppressor APC and Wnt/-Catenin signaling
( www.wormbook.org/chapters/www_cellcyclereguln/cellcyclereguln.html)
Unit VI:
Signal transduction in Health and Disease: Cancer, Neurodegeneration, Diabetes and
Obesity and Inflammation
Recommended Books:
1) Molecular biology- David Freifelder, Narosa Publishing House Pvt. Limited, 2005
2) Biochemistry of Signal Transduction and Regulation. 3rd Edition. Gerhard Krauss,
2003 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ISBN: 3-527-30591-2
3) Molecular Biology of the Cell, 4th edition, Bruce Alberts. New York: Garland
Science; 2002. ISBN-10: 0-8153-3218-1ISBN-10: 0-8153-4072-9
4) Molecular Cell Biology, 4th edition, Harvey Lodish.New York: W. H. Freeman;
2000. ISBN-10: 0-7167-3136-3
5) Principles of cell and molecular biology- Lewis Kleinsmith, 2nd edition, illustrated,
HarperCollins, 1995.
COURSE OUTCOME:
i) Help understand the key principles of biochemical metabolic concepts
ii) Students will learn the signalling pathways that will help them in further studies.
iii) Students learn the basic need of the signalling molecules and the consequesnce on
their absence.
iv) Students will be exposed to most of the actions of the biological system,which they
will study in depth with signalling molecules.
v) Students can able to understand the function of specific anabolic and catabolic
pathways and how these pathways are controlled and interrelated
vi) How current research has provided us with an understanding of the molecular basis of
the control of metabolism
vii) "How to communicate scientific information effectively in writing Hypothesis-based
experimental design"
viii) The course aims to give participants a basic knowledge of mechanisms of signal
transduction and the significance of signal transduction in physiology and
pathophysiology.
BC 202 - INTERMEDIARY METABOLISM
(Core 7)
SEM: II Lecture/Week: 6
BC202 Credits: 6
Objectives
i. To learn the metabolism and integration of biomolecules that takes place in human
system.
ii. Integrate the various aspects of metabolism & their regulatory pathways
iii. Students can understand the fundamental energetics of biochemical processes
iv. To elaborate the relation between biochemical defects and metabolic disorders.
v. To follow the organization of signaling pathways.
Unit - I
Introduction - Overview of major classes of biomolecules, forces stabilizing biomolecules.
General scheme of metabolism, historical and experimental details in derivation of a
metabolic pathway, catabolic, anabolic and amphibolic pathways. Thermodynamics and
metabolism: Cell bioenergetics, laws of thermodynamics, standard free energy, enthalpy,
entropy. Exergonic and endergonic reactions.Definiton of open, closed and isolated system –
Oxidative phosphorylation. Electron transport chain. Standard free energy change of a
chemical reaction, redox potentials, ATP and high energy phosphate compounds.(Blended
Mode of teaching)
Unit - II
Carbohydrates metabolism : Glycolysis and gluconeogenesis – pathway, key enzymes and
co-ordinate regulation.The citric acid cycle and its regulation.The pentose phosphate
pathway.Metabolism of glycogen and regulation.Key junctions in metabolism– glucose-6-
phosphate, pyruvate and acetyl CoA.Blood glucose homeostasis– role of tissues and
hormones.(chalk and talk)
Unit - III
Amino acid metabolism: biosynthesis and degradation of amino acids and their regulation.
Transamination and deamination, ammonia formation, the urea cycle and regulation of
ureogenesis.
Unit IV
Lipids metabolism : Lipogenesis: biosynthesis of fatty acid, triglycerides, phospholipids,
and cholesterol. Regulation of triacylglycerol, phospholipids and cholesterol
biosynthesis.Oxidation of lipids.Role of carnitine cycle in the regulation of β -oxidation.
Ketogenesis and its control.Lipoprotein metabolism - exogenous and endogenus pathways.
Unit - V
Nucleic acid metabolism- biosynthesis and catabolism of purines and pyrimidines and their
regulation.( https://www.slideshare.net/senchiy/nucleic-acids-and-nucleotide)
Unit VI:
Bioenergies in metabolism: High energy phosphates. Components of Electron Transport
chain and the sequence of electron transport. Mechanism of ATP synthesis; Oxidative
phosphorylation – the chemiosmotic theory. Uncoupling of oxidative phosphorylation.
Inhibitors of respiratory chain and oxidative phosphorylation. Mitochondrial transport
systems, ATP/ADP exchange, malate/glycerol phosphate shuttle.
Recommended Books:
7) Biochemistry – L. Stryer.
8) Principles of Biochemistry – R. Horton et al.
9) Lehninger’s Principles of Biochemistry - D. L. Nelson and M. M. Cox.
10) Harpers Biochemistry- R. K. Murray et al.
11) Principles of Biochemistry- G. L. Zubay.
12) Outlines of biochemistry- Lippincott.
COURSE OUTCOME:
i) To learn the metabolism and integration of biomolecules that takes place in human
system.
ii) Integrate the various aspects of metabolism & their regulatory pathways
iii) Students can understand the fundamental energetics of biochemical processes
iv) To understand the relation between biochemical defects and metabolic
disorders.
v) To understand the organization of signaling pathways.
vi) To understand the role of membrane processes in metabolism
vii) Overall, gaining an understanding of the processes of metabolic transformation at the
molecular level and how these processes are studied.
viii) Afford students opportunity to appreciate the relevance/applications of biochemistry in
our daily activities.
Elective Paper – I
BC203 - ECOLOGY AND ENVIRONMENTAL BIOLOGY
(Elective 1)
SEM: II Lecture/Week: 5
BC203 Credits: 3
Objectives
i. To study the physical and biological characters of the environment and the inter-
relationship between biotic and abiotic components of nature as well as
relationship among the individuals of the biotic components.
ii. To understanding of current environmental issues and how global problems affect us
locally
iii. Describe the ecological and evolutionary influence of abiotic factors on organisms
and how these factors affect the distribution and abundance of species.
iv. To understand the core ecological principles, and define scientific principles and
concepts as related to environmental studies and sustainability
v. Students should be able to demonstrate an
vi. Understanding of environmental interrelationships and of contemporary
environmental issues.
Unit - I
The Environment: definition, types of environment and their importance: physical
environment; biotic environment; social environment; biotic and abiotic interactions.
Ecology: scope of ecology; historical background; ecology in India; terminology of ecology;
basic concepts of ecology.(Blended mode of teaching)
Unit - II
Environmental Complex: Environmental and ecological factors-Direct and indirect factors;
four categories of ecological factors-climatic, topographic, edaphic and biotic factors;
interaction of ecological factors. Species Interactions: Types of interactions, interspecific
competition, herbivory, carnivory, pollination, symbiosis. Habitat and Niche: Concept of
habitat and niche; niche width and overlap; fundamental and realized niche; resource
partitioning; character displacement.
Unit - III
Population Ecology: Characteristics of a population; population growth curves; population
regulation; life history strategies (r and K selection); concept of metapopulation – demes and
dispersal, interdemic extinctions, age structured populations. Community Ecology: Nature of
communities; community structure and attributes; levels of species diversity and its
measurement; edges and ecotones. Ecological Succession: Types; mechanisms; changes
involved in succession; concept of climax.
Unit - IV
Ecosystem Ecology: Ecosystem structure; ecosystem function; energy flow and mineral
cycling (C, N, and P); primary production and decomposition; structure and function of
some Indian ecosystems: terrestrial (forest, grassland) and aquatic (fresh water, marine,
eustarine). Biogeography: Major terrestrial biomes; theory of island biogeography;
biogeographical zones of India.(Chalk an talk)
Unit - V
Applied Ecology: Environmental pollution; global environmental change; biodiversity:
status, monitoring and documentation; major drivers of biodiversity change; biodiversity
management approaches. Conservation Biology: Principles of conservation, major
approaches to management, Indian case studies on conservation/management strategy
(Project Tiger, Biosphere reserves).
Unit VI:
Waste Management: Sources, generation, classification & composition of solid wastes. Solid
waste management methods - Sanitary land filling, Recycling, Composting, Vermi-
composting, Incineration, energy recovery from organic waste. Hospital Waste
Management, Hazardous Waste Management & Handling rules, 1989 & 2000
(amendments).( www.businessdictionary.com/definition/waste-management.html)
Recommended Books:
1. Ecology and Environment - PD. Sharma, Rastogi Publications, 7th edition (2007).
2. Ecology-from individuals to ecosystems – Michael Begon, Colin R, Townsend and
John L Harper, Blackwell publishing - 4th edition (2006)
3. Ecology-the plants, animals and the environment-Michael Allaby, Facts on file 1st
edition (2009)
4. Ecology-Robert E Ricklefs, W.H.Freeman Publisher, Fourth edition (2000)
COURSE OUTCOME:
1. To study the physical and biological characters of the environment and the
inter-relationship between biotic and abiotic components of nature as well as
relationship among the individuals of the biotic components
2. To understanding of current environmental issues and how global problems
affect us locally.
3. Describe the ecological and evolutionary influence of abiotic factors on
organisms and how these factors affect the distribution and abundance of
species.
4. To understanding of core ecological principles, and define scientific
principles and concepts as related to environmental studies and sustainability.
5. Students should be able to demonstrate an understanding of environmental
interrelationships and of contemporary environmental issues.
6. To study the extinct species and the cause related to it.
7. Students will able to differentiate the past world environment with the present
and will think on evolution.
8. Students will learn at the end of the course to conserve the nature and will be
able to develop new strategies to preserve the sources of life.
BC204 - LABORATORY COURSE II
(Core 8)
SEM: II Lecture/Week: 6
BC204 Credits: 6
Objectives
i. Extract gene sequence data from public databases, apply principles of gene structure
and expression to identify features within gene sequence, and analyze gene
sequence manually using online software tools
ii. Interpret and discuss the outcome of experiments formally through oral presentations
and written reports
iii. independently clone any gene into a plasmid vector (from RNA extraction, reverse
transcription, polymerase chain reaction, ligation, bacterial transformation, to DNA
extraction, DNA mapping and primer design)
iv. transfect plasmids and silencing RNAs to over-express or knock down protein
expression in a primary cell line, extract protein, assess and quantify expression
using Western blotting
v. Students learn to handle all the equipment regularly that used in DNA manipulation,
including balances, pipettes, electrophoresis and centrifuges and thereby obtain
basic laboratory skills.
1. Cell culture equipment and safety
2. Sterile and Aseptic techniques
3. Cell line repository
4. Preparation of Media for Animal Cell Culture
5. Plating cells from frozen stock
6. Sub culturing adherent Animal cells in culture
7. Cryopreservation and Storage of Animal Cells
8. Determination of Contamination in culture lab and cells
9. Counting cells using a hemocytometer
10. Assessment of Cytotoxicity assay
11. Estimation of total RNA and cDNA synthesis
12. Reverse transcriptase Polymerase chain reaction
COURSE OUTCOME:
1. Extract gene sequence data from public databases, apply principles of gene structure and
expression to identify features within gene sequence, and analyze gene sequence manually
using online software tools.
2. Interpret and discuss the outcome of experiments formally through oral presentations and
written reports.
3. Independently clone any gene into a plasmid vector (from RNA extraction, reverse
transcription, polymerase chain reaction, ligation, bacterial transformation, to DNA
extraction, DNA mapping and primer design).
4. Transfect plasmids and silencing RNAs to over-express or knock down protein expression
in a primary cell line, extract protein, assess and quantify expression using Western blotting.
5. Students learn to handle all the equipment regularly that used in DNA manipulation,
including balances, pipettes, electrophoresis and centrifuges and thereby obtain basic
laboratory skills.
6. To obtain basic laboratory skills such as microscopy, spectrophotometry, measuring, etc.
7. The ability to apply lecture concepts in a laboratory setting.
8. The ability to write scientific reports including analysis of data and graphing.
BC2ED - GENETICS (ED PAPER)
(Non Major Elective I)
SEM: II Lecture/Week: 3
BC2ED Credits: 2
Objectives
i. Identify and describe the process and purposes of the cell cycle, meiosis, and mitosis,
as well as predict the outcomes of these processes.
ii. Transmission genetics problems, make accurate predictions about inheritance of
genetic traits, and map the locations of genes
iii. To identify the parts, structure, and dimensions of DNA molecules, RNA molecules,
and chromosomes, and be able to categorize DNA as well as describe how DNA
is stored
iv. To describe what causes and consequences of DNA sequence changes and how cells
prevent these changes, as well as make predictions about the causes and effects
of changes in DNA
v. To describe applications and techniques of modern genetic technology, as well as
select the correct techniques to solve practical genetic problems
Unit - I
Introduction to Genetics: Brief history/basic concepts of genetics, Cell division and
chromosomes. Mendelian genetics/monohybrid, dihybrid cross. Mendelian
genetics/trihybrid cross, probability. Modification of Mendelian ratios/incomplete and
codominance.Modification of Mendelian ratios/incomplete and codominance.Structure of
Gene - Interaction of Gene - Commentary Factors, Supplementary Factors, Inhibitory and
Lethal Factors - Atavism. (https://www.slideshare.net/vanessaceline/intorduction-to-
genetics)
Unit - II
Diploid chromosomes number- Sex differentiation and sex determination.The X
chromosomes, Barr bodies, the Lyon hypothesis. Aneuploidy and polyploidy: Gene deletion,
duplication, inversions and translocation. Sex Linkage in Drosopohila and Man, Sex
Influenced and Sex Limited Genes - Non-Disjunction and Gynandromorphs - Cytoplasmic
Inheritance - Maternal Effect OnLimnaea (Shell Coiling), Male Sterility (Rode's
Experiment).CO2 sensitivity In Drosophila, Kappa particles in Paramecium, Milk Factor in
Mice.(Blended mode of teaching)
Unit- III
Blood Groups and their Inheritance in Human - Linkage and Crossing Over:- Drosophila -
Morgans' Experiments - Complete and Incomplete Linkage, Linkage Groups, Crossing Over
types, Mechanisms - Cytological Evidence for Crossing Over, Mapping of Chromosomes -
Interference and Coincidence.
Unit IV:
Nature and Function of Genetic Material - Fine Structure of the Gene - Cistron, Recon,
Muton - Mutation - Molecular Basis of Mutation, Types of Mutation, Mutagens, Mutable
and Mutator Genes. Chromosomal Aberrations - Numerical and Structural Examples from
Human.
Unit V:
Applied Genetics – Animal Breeding - Heterosis, Inbreeding, Out Breeding, Out Crossing,
Hybrid Vigour. Population Genetics, Evolutionary genetics, Hardy Weinberg Law - Gene
Frequency, Factors Affecting Gene Frequency, Eugenics, Euphenics and Euthenics,
Bioethics. (www.goldiesroom.org/...)
Unit VI:
Genetic Principles and their application in medical practice; Case studies (Interacting with
patients, learning family history and drawing pedigree chart); Syndromes and disorders:
definition and their genetic basis - Cystic fibrosis and Tay Sach’s Syndrome;
Phenylketonuria and Galactosemia; Ethical issues with clinical genetics.
Recommended Books:
1. Genetics by Verma, P.S. and V. K.Aggarwal.
2. Genetics by Russell P.J.
3. Genetics analysis and principles by Brooker R.J and McGraw Hill.
4. Basic Genetics my Miglani G.S.
5. Genetics: Analysis of genes and genomes by Hartl D.L and Jones E.W.
COURSE OUTCOME:
1.Identify and describe the process and purposes of the cell cycle, meiosis, and
mitosis, as well as predict the outcomes of these processes.
2.Transmission genetics problems, make accurate predictions about inheritance of
genetic traits, and map the locations of genes.
3.To identify the parts, structure, and dimensions of DNA molecules, RNA
molecules, and chromosomes, and be able to categorize DNA as well as describe how DNA
is stored.
4.To describe what causes and consequences of DNA sequence changes and how
cells prevent these changes, as well as make predictions about the causes and effects of
changes in DNA.
5.To describe applications and techniques of modern genetic technology, as well as
select the correct techniques to solve practical genetic problems.
6.To carry out genetics laboratory and field research techniques.
7.To describe experimental results in written format both informally and in formal
manuscript format.
8.To accurately diagram and describe the processes of replication, transcription,
translation, as well as predict the outcomes of these processes"
BC301-IMMUNOLOGY
(Core 9)
SEM: III Lecture/Week: 6
BC301 Credits: 6
Objectives
i. Describe the basic mechanisms, distinctions and functional interplay of innate and
adaptive immunity
ii. Define the cellular/molecular pathways of humoral/cell-mediated adaptive responses
iii. Define the basic mechanisms that regulate immune responses and maintain tolerance
iv. To demonstrate the molecular basis of complex, cellular processes involved in
inflammation and immunity, in states of health and disease.
v. Describe basic and state-of-the-art experimental methods and technologies
Unit - I
Historical perspective: contribution by metchinikoff, Edward Jenner, Louis Pasteur and
Wu and Kabat. Types of immunity – innate and acquired. Humoral and cell mediated
immunity. Central and peripheral lymphoid organs – Thymus, bone marrow, spleen, lymph
nodes and other peripheral lymphoid tissues – MALT, GALT and CALT. Cells of the
immune system- lymphocytes, mononuclear phagocytes – dendritic cells, granulocytes, NK
cells and mast cells.Immunoglobulins – structure, classification and functions. Idiotype
network hypothesis. Antigen, types of antigen, antigen Vsimmunogens, Haptens. Factors
influencing immunogenicity.Isotypes, allotypes and idiotypes.(Blended mode of teaching)
Unit - II
Complement system: components of complement activation and its biological consequences
– classical, alternative and lectin pathways. Clonal selection theory.Organization and
expression of immunoglobulin genes, generation of antibody diversity.Class switching.
Overview of B cell & T cell, types of immune response, T – cell, B- cell receptors, Antigen
recognition – processing and presentation to T- cells. Interaction of T and B cells.Effector
mechanisms – macrophage activation. Cell mediated cytotoxicity, Cytokines types,
regulation of immune response : immune tolerance and immunosuppression.(Chalk and
talk)
Unit - III
Major Histocompatibility complex (MHC): MHC genes and products. Polymorphism of
MHC genes, role of MHC antigen in immune response, MHC antigens in transplantation.
Transplantation types, allograft rejection mechanism. Immune response to infectious
diseases – Viral, bacterial and protozoal.AIDS and other immunodeficiency disorders.
Autoimmunity: Mechanism of induction of organ specific and systemic auto immune
diseases. Hypersensitivity – types. Immune response to cancer, immunotherapy.
Unit IV
Immunization practices – active and passive immunization. Vaccines – killed, attenuated –
toxoids. Recombinant vector vaccines – DNA vaccines, synthetic peptide vaccines – anti
idiotype vaccines.Humanized antibodies and plantibodies.Production of polyclonal and
monoclonal antibodies.Principles, techniques and application.Genetically engineered
antibodies.Abzymes.
Unit V
Immunotechniques: Agglutination and precipitation technique. Immuno – electrophoresis,
RIA, immunoblotting, Avidin – biotin mediated immune assay. Immunohistochemistry –
immunofluorescence, immune ferritin technique. Fluorescent immunoassay, fluorescence
activated cell sorting (FACS). Cytokines assay: ELISA and ELISPOT. Lymphocytes
transformation test (LTT); Lymphoblastoid cell lines. Experimental animal models: inbred
strains, SCID mice, nude mice, knockout mice fully cloned animals.
(www.biologydiscussion.com/biochemistry/immunochemical...)
Unit VI:
Recent studies on Auto-immune disorders, Hypersensitivity. Dynamics of the
immune response. The immune response in health and disease.
Recommended Books:
1. Geoffrey Zubay - (1972), Immunology, 4thedition, W.M.C. Brown publishers.
2. Janis Kuby - (1997), immunology, 3rdedition, W.H. Freedom & co (Sd).
3. Kenneth M. Murphy, Paul Travers, Mark Walport - (2007),
Janeway’simmunobiology, 7thedition, Garland Science.
4. Peter Delves, Seamus Martin, Dennis Burton, Ivan Roitt - (2006),Roitt's
EssentialImmunology, 11th edition, Wiley-Blackwell.
5. Abul K. Abbas, Andrew H. Lichtman, Jordan S. Pober - (1994), Cellular and
molecular immunology, 2ndedition, B. Saunders Company.
6. Donald Mackay Weir & Stewart John - (1997), Immunology, 8th edition, Churchill
Livingstone.
COURSE OUTCOME
1. Describe the basic mechanisms, distinctions and functional interplay of innate
and adaptive immunity.
2. Define the cellular/molecular pathways of humoral/cell-mediated adaptive
responses.
3. Define the basic mechanisms that regulate immune responses and maintain
tolerance.
4. Understand the molecular basis of complex, cellular processes involved in
inflammation and immunity, in states of health and disease .
5. Describe basic and state-of-the-art experimental methods and technologies .
6. Integrate knowledge of each subsystem to see their contribution to the
functioning of higher-level systems in health and disease.
7. Apply understanding of basic and state-of-the-art experimental methods and
technologies in the design of research plan to test specific hypotheses.
8. Translate understanding of basic mechanisms into identification of biological,
clinical and therapeutic implications.
BC302 - GENETIC ENGINEERING AND MOLECULAR
TECHNIQUES
(Core 10)
SEM: III Lecture/Week: 6
BC201 Credits: 6
Objectives
i. This course is to discipline to students knowledge of main engines of implementation
and transmission of a genetic material at molecular and cellular levels
ii. The methods of change of a genetic material and constructioning of transgene
organisms with the given properties.
iii. Students can be understand Know the natural function of restriction endonucleases
and how a normal bacterial cell protects its DNA from their activity
iv. Understand the value of and the processes involved with the polymerase chain
reaction (PCR).
v. To understand the function of creative use of modern tools and techniques for
manipulation and analysis of genomic sequences
Unit - I
Introduction to gene cloning: Restriction and modification enzymes. Cloning vectors:
Characteristics, Natural & artificial plasmids as vectors - advantages and disadvantages.
Vectors used for cloning in E.coli., yeast, higher plants (Ti plasmid derivatives,
caulimovirus) and animal cells (constructs of SV 40 and retroviruses). Characteristics of
expression vectors. Construction of DNA libraries - genomic and cDNA libraries. Screening
of recombinants.(Blended of teaching)
Unit - II
Transposons and transposable elements: Transgenic animals - Gene transfer methods in
animals. Recombinant selection and screening. Totipotency, haploids, growth of animal cell
lines. Competent cells preparation, electroporation, microinjection and particle
bombardment method, and selection of transformants. Transgenic plants - Use of
agrobacterium for genetic engineering in plants. Plant cell cultures for the production of
important compounds. Plant tissue culture – Micropropagation, protoplast isolation, somatic
hybrids. Identification of transformed cells into callus and regeneration of transgenic plants
Unit - III
Molecular techniques: Polymerase chain reaction – principle, types and applications.
Sanger’s and Maxam-Gilbert’s method for DNA sequencing. DNA Finger Printing - RAPD,
RACE (Rapid Amplification of cDNA Ends), RFLP and AFLP analysis and its application
in forensic science, pedigree analysis, biodiversity, genetic counselling and germplasm
maintenance. DNA foot printing. Chromosome walking, chromosome jumping.
Mutagenicity test – Ames test. Markers linked to drug and disease resistant genes. Antisense
technology and its application. Microarray technology: genomic and cDNA arrays.(
https://www.slideshare.net/drmalathi13/molecular-techniques)
Unit- IV
Gene therapy: Ex-vivo, Invivo, Insitu gene therapy Stratagies of gene therapy: Gene
augmentation – ADA defeiciency, CFTR, Antisense therapy, Ribozymes, Protein Aptamers,
Intrabodies. Stem cell therapy - Embryonic and adullt Stem Cells, Totipotent, Pluripotent
and Mulltipotent Cells. Testing and generation of embryonic stem cells, Testing for adult
stem cells and differentiation, Potential use of stem cells – Cell based therapies.
Unit –V
Human genome projects, gene bank. Genetically modified organisms (GMOs) in developed
and developing countries. Genetically modified foods – benefits and risks. Bioethics: Laws
and regulations in biotechnology, patent laws, and Intellectual property rights (IPR).
Biosafety, types of biosafety, advantage and disadvantage.Ethics in cloning and stem cell
research.
Unit VI:
Genetics of Metamorphosis, Regeneration & Aging – Compensatory regeneration in the Mammalian
Liver, Causes of Aging, Genetically regulated pathway of Aging. (chalk and talk)
Recommended Books:
1. Molecular Cloning: A Laboratory manual, J. Sambrook, E.Ffrisch and T. Maniatis,
Old Spring Harbor Laboratory Press New York, 2000
2. DNA Cloning : a Practical Approach, DM Glover and BD Hames, IRL Press
3. Molecular and Cellular methods in Biology and Medicine. PB Kaufman,W.Wu.D
Kim and LJ Cseke, CRC
4. DNA Science. A first Course in Recombinant Technology, DA Mickloss and GA
Freyer, Cold Spring Harbor Laboratory Press, New York 1990
5. Molecular Biotechnology (2nd Edn) SB Primrose, Blackwell Scietific Pub. Oxford,
1994
6. Milestones in Biotechnology. Classic papers on Genetic Engineering. JA Davies and
WS Reznikoff, Butterworth-Heinemann, Boston, 1992
7. Route Maps in Gene Technology, MR Walker and R Rapley, Blackwell Science Ltd,
Oxford 1997
8. Molecular Biotechnology. Glick
9. Principles of Gene Manipulation by Old and Primrose, Blackwell publications
COURSE OUTCOME
1. This course is to discipline to student’s knowledge of main engines of
implementation and transmission of a genetic material at molecular and cellular
levels.
2. The methods of change of a genetic material and constructing of transgene organisms
with the given properties.
3. Students can be understood Know the natural function of restriction endonucleases
and how a normal bacterial cell protects its DNA from their activity.
4. Understand the value of and the processes involved with the polymerase chain
reaction (PCR).
5. To understand the function of creative use of modern tools and techniques for
manipulation and analysis of genomic sequences.
6. This technique can use to train students in strategizing research methodologies
employing genetic engineering techniques.
7. Understand the similarities and differences between how genetic information is
passed on in eukaryotes and prokaryotes.
8. Students can observe the Identify the fundamental differences between genetically
engineered crops and non-genetically engineered crops.
BC303 - CLINICAL BIOCHEMSITRY
(Elective 2)
SEM: III Lecture/Week: 5
BC303 Credits: 3
Objectives
i. An advanced understanding and applied knowledge of the theory and practice of
clinical biochemistry;
ii. The student will be able to describe the structure, function and metabolic pathways
for carbohydrates, amino acids and lipids.
iii. To learn the alterations in lipid and carbohydrate metabolism that occur as a result of
diabetes.
iv. To make the students biochemistry of membranes including chemical composition
and structure of biological membranes, as well as drug transporters
v. To impart thorough knowledge about the biochemical basis of various diseases and
disorders
Unit- I
Introduction to Biochemical laboratory: Roles of biochemical laboratory. Mechanization
and amomation in clinical biochemistry. Quality control in clinical laboratories. Total
laboratory uncertainty. Accuracy and precision. Selection and optimization of laboratory
methods, Clinical evaluvation of laboratory methods.
Biochemical analysis in urine. Clinical biochemical analysis of proteins. Plasma protein
spectrum during inflammation, paraproteins. Blood gases. Electrolytes and acid – base
balance. Regulation of electrolyte content of body fluids and maintenance of pH
reabsorption of electrolytes. Acidosis & Alkaloids and their determination in clinical
laboratory.(chalk and talk)
Unit- II
Disorder of carbohydrate metabolism: Diabetes mellitus, classification, etiology,
management, laboratory investigations- GTT. HB Alc. Diabetic complications, sugar levels
in blood, threshold for glucose, factors influencing blood glucose level. Glycogen storage
diseases, pentosuria, and galactosemsia.
Disorder of protein metabplism: Alpha – fectoprotein, Amyloidosis. Cryoglobulinaemia.
Hypo and hyper immunogammaglobulinaemia.
Unit III
Disorders of lipids: Plasma lipoproteins, cholesterol, triglycerides & phospholipids in
health and disease. Hyperlipidemia, hyperlipoproteinemia.Gauchers disease. Tay – sachs and
Niemann – Pick disease, ketone bodies. Abetalipoproteinemia. Major Cardio vascular
diseases – Atheroschrosis – risk factors, pathogenesis. Laboratory diagnosis of acute
myocardial infraction.( www.med.muni.cz/patfyz/pdf/new/met)
Inborn error of metabolism: Phenylketonuria, alkaptonuria, albinism, tyrosinosis, mape
syrup urine disease. Leish – Nyhan syndrome, sikle cell anemia.Histidinemia. Abnormalities
in Nitrogen Metabolism Uremia., porphyria and factors affecting nitrogen balance.
Unit IV
Disoders of liver kidney: Biochemical indices of hepatobiliary disease. Bile pigments –
formation of bilirubin, urobilinogen bile acids, jaundice – prehapic, hepatic and posthepatic.
Fatty liver, normal and abnormal functions of liver. Liver function tests, diseases of the liver
– hepatitis, cholestasis, cirshosis. Gallstones. Diagnostic Enzymes – Enzymes in health and
diseases. Disoders of kidney: Assessment of renal function – creatine clearance, renal
calculi, uremia and laboratory investigation of kidney disorders, renal function tests.
Unit V
Circulation disorders: Composition cells, functions of plasma proteins and lipoproteins in
diseases. Disorders of haemoglobin – thalassemia, sickle cell anemia – Microcytic,
normocytic and macrocytic anemias. Endocrine disorders: Pituitary, thyroid, adrenals and
gonads- hypo and hyper secretion of hormones. Disorders – Graves diseases and Addition
diseases.(Blended mode of teaching)
Unit VI:
Diagnosis and interpretation: Evaluation and clinical significance of: Blood gases, Various
electrolytes (Na+, K+, HCO3, etc), Urea, Uric acid. Enzymes; Alkaline phosphatase,
Alanine aminotransferase, Aspartate aminotransferase, Lactate dehydrogenase, Creatine
kinase, Amylase, Lipase. Insulin tolerance test; growth hormone stimulation test;
Adrenocorticotropin, congenital adrenal hyperplasia or hirsutism.
Recommended Books:
a. Rodney F. Boyer - (2010). Biochemistry Laboratory: Modern Theory and Techniques,
2thedition, Pearson Prentice Hall.
b. Undurti N. Das - (2011). Molecular Basis of Health and Disease, 1st edition,Springer.
c. Nanda Maheshwari – (2008). Clinical biochemistry, 1st edition, JAYPEE.
d. MN Chatterjea, Ranashinde – (2012). Textbook of Medical Biochemistry, 8th edition,
JAYPEE.
e. By William J. Marshall, S. K. Bangert – (1995). Clinical Biochemistry: Metabolic and
Clinical Aspects, 1st edition, Churchillivingstone.
f. Michael Lieberman, Allan D. Marks – (2009). Marks' Basic Medical Biochemistry: A
Clinical Approach, 3rd edition,Lippincott Williams & Wilkins.
g. Miriam D. Rosenthal, Robert H. Glew – (2009). Medical Biochemistry: Human
Metabolism in Health and Disease, 1st edition, Wiley.
COURSE OUTCOME
1. An advanced understanding and applied knowledge of the theory and practice of
clinical biochemistry.
2. The student will be able to describe the structure, function and metabolic pathways
for carbohydrates, amino acids and lipids.
3. To learn the alterations in lipid and carbohydrate metabolism that occur as a result of
diabetes.
4. Explain the metabolism of lipoproteins, medical problems associated with abnormal
lipoprotein levels and therapeutic agents used to treat lipid disorders.
5. To make the students biochemistry of membranes including chemical composition
and structure of biological membranes, as well as drug transporters.
6. To impart thorough knowledge about the biochemical basis of various diseases and
disorders.
7. To study various diagnostic and therapeutic methodologies available for diseases and
disorders. Students can apply biochemistry concepts to solve clinical scenarios.
8. Describe intercellular and intracellular signal transductions and explain the molecular
mechanism of drug actions.
BC304 - LABORATORY COURSE III
(Core 11)
SEM: III Lecture/Week: 6
BC304 Credits: 4
Objectives
i. The overall aim of this course is that the student should gain a basic working
knowledge SDS PAGE, WESTERN BLOTTING techniques.
ii. This course helps in enhancing students skill in molecular techniques which will help
them to fetch projects outside the department
iii. The student would able to describe the priciples and methods almost all the molecular
techniques.
iv. Students will be exposed to instruments used in molecular study.
v. Aims to Develop critical thinking skills/ laboratory techniques so as to be capable of
designing, carrying out, interpreting scientific experiments
1. Deriving Gene sequence from N BLAST
2. Designing primers, online software for primer design
3. Gradient PCR
4. Agarose gel
5. Isolation of plasmid DNA
6. Digestion of plasmid with restriction enzyme
7. DNA ligation
8. Transformation of plasmid construct to vector cells
9. DNA and protein over expression
10. SDS-PAGE Electrophoresis
11. Western blot
12. Assay of Alkaline phosphatase activity
13. Effect of pH and Temperature on enzyme activity
14. Determination of Vmax and Km for enzyme activity
COURSE OUTCOME:
1.The overall aim of this course is that the student should gain a basic working
knowledge SDS PAGE, WESTERN BLOTTING techniques.
2.This course helps in enhancing students skill in molecular techniques which will
help them to fetch projects outside the department
3.The student would able to describe the priciples and methods almost all the
molecular techniques.
4.Students will be exposed to instruments used in molecular study.
5.Aims to Develop critical thinking skills/ laboratory techniques so as to be capable
of designing, carrying out, interpreting scientific experiments.
6.Students will use current biochemical and molecular techniques to plan and carry
out experiments. They will generate and test hypotheses, analyze data using statistical
methods where appropriate, and appreciate the limitations of conclusions drawn from
experimental data. Trouble-shooting will be stressed in classes and labs.
7.Students will be knowledgeable in proper procedures and regulations in handling
and disposal of chemicals. Assessment of this learning outcome occurs in every laboratory
course.
8.Students will learn to design a Primer, basics of proteiomics and genomics.
BC3ED - DEVELOPMENTAL BIOLOGY
(Non major 2)
SEM: III Lecture/Week: 3
BC3ED Credits: 2
Objectives
i. To understand the molecular and cellular mechanisms of development and learn
about basic embryology
ii. To understanding the students will be able to generally describe the concepts of
cellular competence, induction, specification, commitment and differentiation in
embryonic development.
iii. To recognize the how to explain at least two concepts in developmental biology that
overlap with other sciences, such as stem cell research, cancer research, evolutionary
sciences, or neuroscience.
iv. Students will be able to discern and summarize the current state of knowledge on a
given topic, construct pioneering research questions on that topic, and propose
experiments aimed at answering those questions.
v. To make the students how the knowledge in genetics, evolutionary biology, cell
biology, developmental biology, physiology and ecology.
Unit- I
Emergence of evolutionary thoughts: Lamarks; Darwin – concepts of variation,
adaptation, struggle, fitness and natural selection; Mendelism; spontancity of mutations; the
evolutionary synthesis, Origin of cells and unicellular evolution; Origin of basic biological
molecules; abiotic synthesis of organic monomers and polymers; concept of Oparin and
Haldane; experiment of Miller (1953); the first cell; evolution of prokaryotes; origin of
eukaryotic cells; evolution of unicellular eukaryotes; anaerobic metabolism, photosynthesis
and aerobic metabolism.
Unit - II
Basic concepts of development: Potency, commitment, specification, induction,
competence, determination and differentiation; morphogenetic gradients; cell fate and cell
lineages; stem cells; genomic equivalence and the cytoplasmic determinants; imprinting;
mutants and transgenics in analysis of development.( cmb.i-
learn.unito.it/mod/book/tool/print/index.php)
Unit - III
Gametogenesis, Fertilization and early development: Production of gametes, cell surface
molecules in sperm-egg recognition in animals; embryo sac development and double
fertilization in plants; zygote formation, cleavage, blastula formation,embryonic fields,
gastrulation and formation of germ layers in animals; embryogenesis, establishment of
symmetry in plants; seed formation and germination.(Blended mode)
Unit - IV
Morphogenesis and organogenesis in animals: Cell aggregation and differentiation in
Dictyostelium; axes and pattern formation in Drosophila, organogenesis – vulva formation
in Caenorhabditiselagans; eye lense induction, limb development and regeneration in
vertebrates; differentiation of neurons, post embryonic development- larval formation,
metamorphosis; environmental regulation of normal development; sex determination.
Unit V:
Morphogenesis and organogenesis in plants: Organization of shoot and root apical
meristem; shoot and root development; lead development and phyllotaxy; transition to
flowering, floral development in Arabidopsis and Antirrhunum.(Chalk and talk)
Unit VI:
Medical implications of developmental biology-genetic errors/ teratogenesis/ stem cell
therapy.
Recommended Books:
1. Principles of Development. 3rd edition, by L. Wolpert, 2006, Oxford University
press, incorporated.
2. Developmental Biology. 3rd edition, by Lewis Wolpert, 2006, Oxford University
Press, USA
3. Developmental Biology, 6th edition by Scott Gillbert, 2000, Sunderland
(MA): Sinauer Associates; ISBN-10: 0-87893-243-7
4. Evolutionary developmental biology, 2nd edition by Brain K. Hall. 1998,
Springer;ISBN-10: 0412785803
COURSE OUTCOME:
1. To Understand the molecular and cellular mechanisms of development and
learn about basic embryology
2. To understanding the students will be able to generally describe the concepts
of cellular competence, induction, specification, commitment and
differentiation in embryonic development.
3. To understand the how to explain at least two concepts in developmental
biology that overlap with other sciences, such as stem cell research, cancer
research, evolutionary sciences, or neuroscience.
4. Students will be able to discern and summarize the current state of knowledge
on a given topic, construct pioneering research questions on that topic, and
propose experiments aimed at answering those questions.
5. To make the students how to understand the knowledge in genetics,
evolutionary biology, cell biology, developmental biology, physiology and
ecology.
6. It is useful for awareness of scientific methods and research skills used to
investigate cell & developmental biology problems
7. To awareness of ethical issues in cell and developmental biology research,
particularly in relation to stem cells, in vitro fertilisation and assisted
reproductive technologies.
8. Students can understand the capacity to evaluate and synthesise information
from a wide range of sources in order to communicate ideas, concepts and
construct arguments in both non-scientific and scientific language.
PROJECT DISSERTATION
SEM: III Lecture/Week:
30
BC401 Credits: 20
Each candidate shall be required to take up a Project Work; submit Project Report at
the end of the second year. The Head of the Department shall assign the Guide who in
turn will suggest the Project Work to the student in the beginning of fourth semester.
Two typed copies of the Project Report shall be submitted to the Department on or
before the date fixed by the Department Head.
The Dissertation will be evaluated by Examiners, nominated by the Department. The
candidate concerned will have to defend his project in a Viva-Voce examination
ELECTIVE PAPERS I & II
BC203 - ECOLOGY AND ENVIRONMENTAL BIOLOGY (ELECTIVE)
Objectives:
To study the physical and biological characters of the environment and the inter-
relationship between biotic and abiotic components of nature as well as relationship among
the individuals of the biotic components
Unit - I
The Environment: definition, types of environment and their importance: physical
environment; biotic environment; social environment; biotic and abiotic interactions.
Ecology: scope of ecology; historical background; ecology in India; terminology of ecology;
basic concepts of ecology.(Flipped mode)
Unit - II
Environmental Complex: Environmental and ecological factors-Direct and indirect factors;
four categories of ecological factors-climatic, topographic, edaphic and biotic factors;
interaction of ecological factors. Species Interactions: Types of interactions, interspecific
competition, herbivory, carnivory, pollination, symbiosis. Habitat and Niche: Concept of
habitat and niche; niche width and overlap; fundamental and realized niche; resource
partitioning; character displacement.(Blended mode)
Unit- III
Population Ecology: Characteristics of a population; population growth curves; population
regulation; life history strategies (r and K selection); concept of metapopulation – demes and
dispersal, interdemic extinctions, age structured populations. Community Ecology: Nature of
communities; community structure and attributes; levels of species diversity and its
measurement; edges and ecotones. Ecological Succession: Types; mechanisms; changes
involved in succession; concept of climax.
Unit - IV
Ecosystem Ecology: Ecosystem structure; ecosystem function; energy flow and mineral
cycling (C, N, and P); primary production and decomposition; structure and function of
some Indian ecosystems: terrestrial (forest, grassland) and aquatic (fresh water(, marine,
eustarine). Biogeography: Major terrestrial biomes; theory of island biogeography;
biogeographical zones of India.(https://study.com/academy/lesson/ecosystem-ecology-
definition-lesson)
Unit - V
Applied Ecology: Environmental pollution; global environmental change; biodiversity:
status, monitoring and documentation; major drivers of biodiversity change; biodiversity
management approaches. Conservation Biology: Principles of conservation, major
approaches to management, Indian case studies on conservation/management strategy
(Project Tiger, Biosphere reserves).
Unit VI:
Waste Management: Sources, generation, classification & composition of solid wastes. Solid
waste management methods - Sanitary land filling, Recycling, Composting, Vermi-
composting, Incineration, energy recovery from organic waste. Hospital Waste
Management, Hazardous Waste Management & Handling rules, 1989 & 2000
(amendments).
Recommended Books:
1. Ecology and Environment - PD. Sharma, Rastogi Publications, 7th edition (2007).
2. Ecology-from individuals to ecosystems – Michael Begon, Colin R, Townsend and John
L Harper, Blackwell publishing - 4th edition (2006)
3. Ecology-the plants, animals and the environment-Michael Allaby, Facts on file 1st edition
(2009)
4. Ecology-Robert E Ricklefs, W.H.Freeman Publisher, Fourth edition (2000)
COURSE OUTCOME:
9. To study the physical and biological characters of the environment and the
inter-relationship between biotic and abiotic components of nature as well as
relationship among the individuals of the biotic components
10. To understanding of current environmental issues and how global problems
affect us locally.
11. Describe the ecological and evolutionary influence of abiotic factors on
organisms and how these factors affect the distribution and abundance of
species.
12. To understanding of core ecological principles, and define scientific
principles and concepts as related to environmental studies and sustainability.
13. Students should be able to demonstrate an understanding of environmental
interrelationships and of contemporary environmental issues.
14. To study the extinct species and the cause related to it.
15. Students will able to differentiate the past world environment with the present
and will think on evolution.
16. Students will learn at the end of the course to conserve the nature and will be
able to develop new strategies to preserve the sources of life.
BC205 BIOINFORMATICS
Objective:
i. The purpose of studying this paper is to apply computational facility in different
fields of life sciences, physical and chemical sciences.
ii. After completion, students could learn drug designing through computer based
modification programs using synthetic or natural source.
iii. Most important application of Bioinformatics is in the field of drug discovery where
it reduces more than 60% of the time, money and labor.
Unit-I
Bioinformatics: An overview, Definition & History; Bioinformatics databases & tools on
the Internet- NCBI, EBI, PIR, Swiss-Prot, GenBank ; pattern and motif searches- BLOCKS,
PRINTS, PFAM.( https://www.britannica.com/science/bioinformatics)
Unit-II
Proteins Amino acids: Levels of protein structure – Ramachandran Map. Protein
Secondary structure prediction - Chou-Fasmann rules, Gamier-Osguthorpe-Robson (GOR)
methods; Predicting 3D structure – homology modeling, threading - fold recognition and ab
initio methods - Rosetta – CASP.( Blended mode)
Unit-III
Biological Sequence analysis: Pairwise sequence comparison – Sequence queries against
biological databases – BLAST and FASTA - Multiple sequence alignments –Phylogenetic
alignment.
Algorithms and Matrices: Scoring matrices- PAM and BLOSUM; dynamic programming
Algorithms, Needleman and Wunsch, Smith-Waterman;
Unit-IV
Protein structure visualization tools: RasMol, HEX, Argus Lab Swiss PDB Viewer -
Structure –Classification, alignment and analysis – SCOP, CATH, FSSP, UNIX.(Flipped
mode)
Unit-V
Functional Genomics (Metabolism and Regulation) in Biochemistry : Sequencing
genomes– Genome databases on the web, Prokaryotic Genome Database with comparison
with Human genome, HGP, GENECLUSTER, DNA Microarray, SWISS-2DPAGE
Database, TIGR,WIT, CYTOSCAPE and DRUG DISCOVERY.
Unit VI:
Current Advancements in Bioinformatics: Introduction to System Biology, Structural
Biology, Structural bioinformatics, Chemoinformatics, Immunoinformatics.
Reference Books
1. Bioinformatics-Sequence and Genome Analysis- David W.Mount, Cold Spring Harbor
Laboratory Press (2004).
2. Introduction to Bioinformatics, Attwood, T.K. and D.J. Parry-Smith, Pearson Education
Ltd., New Delhi (2004).
3. Bioinformatics – Westhead, D.R., Paris J.H. And R.M. Twyman, Instant Notes: Viva
Books Private Ltd, New Delhi (2003).
4. Introduction to Bioinformatics, Arthur M. Lesk, Oxford University Press, New Delhi
(2003).
5. Bioinformatics- Sequence, structure and databanks, Higgins D. and W. Taylor (Eds),
Oxford University Press, New Delhi (2000).
6. Bioinformatics; A practical Guide to the Analysis of Genes and Proteins, Wiley-
Interscience, Baxevanis, A. and B.F. Ouellette , Hoboken, NJ (1998).
7. Introduction to computational Biology, Michael, S. Waterman, Chapman & Hall, (1)
COURSE OUTCOME:
1. The student can explain which type of data is available from the most
common protein sequence and structure databases (UniProt, GenBank,
Protein Data Bank, CATH).
2. The candidate can explain the theories underlying the most common
methods for sequence searches and sequence alignments, and in particular
knows the principle and main steps for pairwise and multiple sequence
alignments;
3. The student can explain and is able to apply the main steps of dynamic
programing for/to simple alignments of short sequences;
4. The student can list methods to uncover structure-function relationship in
proteins and knows their underlying principles;
5. The student can explain the principles of computational methods for the
prediction of secondary structure elements from protein sequence,
prediction and modeling of three-dimensional protein structures
(homology modeling, threading and ab initio methods).
6. select and apply the most appropriate bioinformatics sequence or structure
database to retrieve or search data given a specific question in molecular
biology;
7. select and apply the most appropriate method for aligning sequences,
visualizing and analyzing protein structures, predicting secondary
structure elements and modeling protein structures from sequence.
8. Using their theoretical knowledge about the most commonly used
bioinformatics methods, the student is able, if encountering a new online
tool, to get a general understanding of its underlying principle.
BC206 BIOSTATISTICS
Objectives:
The course emphasizes on various statistical methods and its significance.
The students are expected to understand the concepts and solve relevant problems
pertaining to each topic.
To provide sufficient background to be able to interpret statistical results in research.
Unit- I
Statistical survey: Organizing, planning and executing the survey. Source of data - Primary
and secondary data, collection, observation, interview, enquiry forms, questionnaire
schedule and check list. Classification and tabulation of data. Diagrammatic and graphic
presentation of data.(Blended mode of teaching)
Unit-II
Measures of central tendency : Arithmetic mean, median, mode, quartiles, deciles and
percentiles. Measures of variation - range, quartile deviation, mean deviation, standard
deviation, Coefficient of variation. Correlation analysis - Scatter diagram, Karl's Pearson's
coefficient of correlation and Spearman's rank method. Regression analysis.(Problem based
learning)
Unit-III
Probability: Definition, concepts, theorems (proof of the theorems not necessary) and
calculations of probability - Simple problems. Theoretical distributions – Binomial, Poisson
and normal distribution - Simple problems (proof of the theorems not necessary).(problem
based learning)
Unit-IV
Sampling distribution and test of significance: Concepts of sampling, Testing of
hypothesis, errors in hypothesis testing, standard error and sampling distribution, sampling
of variables (large samples and small samples.). Student's "t" distribution and its
applications. Chi-square test and goodness of fit. Analysis of variance - one way and two
way classification. Duncan's Multiple Range test. Design of experiment- Completely
randomized block design, Randomized block design.
Unit-V
Scientific Methodology: Selection of research problems – hypothesis – definition and
characteristics. Experimental approaches – biological, physical and chemical methods.
Sources of information: Journals, e-journals, books, biological abstracts, Preparation of
index cards, Review writing, Article writing – structure of article. Selection of journals for
publication- Impact factor – Citation index and H index. Proposal writing for funding.IPR
and Patenting – Concept and types.
Unit VI:
Basic statistics: Mathematical Expectation and Generating Functions, Definition and
its properties-moments, addition and multiplication, theorem of expectation. Conditional
expectation and conditional variance. Moments generating function, cumulant generating
function, probability, generating function along with their properties.
Reference Books:
1. Statistical Methods, 4th Edition- Gupta, S.P, Sultan Chand & Son Publishers. 2012.
2. Biostatistical Analysis, 5th Edition- Zar, J.H, Pearson Education, 2010.
3. Biostatistics - Daniel, W.W. A Foundation for Analysis in Health Sciences, 10th Edition,
John Wiley and Sons, Inc., 1999.
COURSE OUTCOME:
1. Select from, use and interpret results of, descriptive statistical methods effectively;
2. Demonstrate an understanding of the central concepts of modern statistical theory
and their probabilistic foundation;
3. Select from, use, and interpret results of, the principal methods of statistical inference
and design;
4. Communicate the results of statistical analyses accurately and effectively;
5. Make appropriate use of statistical software.
6. Read and learn new statistical procedures independently
7. The students will be able to estimate and interpret three alternative measures of
association between binary exposures and binary outcomes and discuss the relative
merits of each measure for a given research question.
8. The student can explain the basis of the linear regression model, fit a linear
regression model using standard statistical software, assess the fit of the model, and
interpret the results.
BC207- CHROMATIN AND EPIGENETICS
Objective:
This an elective course for Biochemistry majors. The objective of this course is to
provide students with a solid foundation in both the principles of epigenetics and
experimental research by emphasizing the use of primary research articles and focusing on
developing analytical scientific reading and writing skills to focus on the current questions
in epigenetics and how they are being addressed experimentally.
Unit-I
Chromatin structure: DNA and histones, nucleosome, organization of nucleosome in
chromatin, chromosomal architecture, modulation of chromosome structure, histones,
chromatin and nuclear assembly, transcription in chromatin, chromatin remodeling
machines. (www.abcam.com/epigenetics/chromatin-structure-and-function)
Unit-II
Epigenetics: Introduction to epigenetics, basic concept overview and brief history of the
field, Epigenetic modifications and gene expression: DNA methylation, DNA acetylation,
Lost in translation: Non-coding RNAs in Epigenetics.(Blended mode of teaching)
Unit-III
Linking epigenetic modifications: Chromatin remodelling and transcription, Model animal
systems for studying epigenetic regulation, Genomic imprinting in mammals, multiple layers
of epigenetic regulation; genome-wide analysis of epigenetic markers.
(https://www.whatisepigenetics.com/chromatin-remodeling)
Unit-IV
Epigenetics and the environment: Gene-environment interactions, environmental
epigenomics, interplay of genome rearrangement and environment during development,
Epigenetic programming in cell renewal and pluripotency.
Unit-V
Epigenetics in disease:
Epidemiology of health, epigenetics and endocrine diseases, Environmental
epigenetics and obesity, Epigenetics and cancer, Epigenome and aging, epigenetics and
cardiovascular disease, epigenetics and brain, Epigenetics and microRNA, Epigenetics in
drug discovery.
Unit VI:
The Histone Code: Biochemistry of Modifying Enzymes, Binding Proteins and
RNAs in Chromatin Regulation (protein-protein, protein-nucleic acids interactions, complex
purification)
Text Book:
Chromatin and Gene Regulation: Molecular Mechanisms in Epigenetics by B. M.
Turner (2008)
Reference book:
1. Epigenetics and Chromatin edited by Philippe Jeanteur (2008)
2. Epigenetics: The Death of the Genetic Theory of Disease Transmission by Joel D.
Wallach, Ma Lan, Gerhard N. Schrauzer (2014)
3. epigenetic epidemiology edited by Karin B. Michels - 2012
4. Epigenetics in human diseases edited by Trygve Tollefsbol (2012)
COURSE OUTCOME:
1. Understand differences between Mendelian and epigenetic inheritance
2. Understand DNA methylation regulates gene expression
3. Understand how chromatin modifications and remodelling regulate gene
expression
4. Understand the role of non-coding RNAs in epigenetic regulation
5. Understand how epigenetic modifications are propagated
6. Understand the research process from hypothesis generation to final presentation
of results
7. Be able to generate testable research questions from observations.
8. Be able to design a controlled experiment to test a hypothesis and to present
findings of a primary research paper and indicate their significance/limit
BC303 - CLINICAL BIOCHEMSITRY (ELECTIVE)
Objective
i. An advanced understanding and applied knowledge of the theory and practice of
clinical biochemistry;
ii. The student will be able to describe the structure, function and metabolic pathways
for carbohydrates, amino acids and lipids.
iii. To learn the alterations in lipid and carbohydrate metabolism that occur as a result of
diabetes.
iv. To make the students biochemistry of membranes including chemical composition
and structure of biological membranes, as well as drug transporters
v. To impart thorough knowledge about the biochemical basis of various diseases and
disorders
Unit -I
Introduction to Biochemical laboratory: Roles of biochemical laboratory. Mechanization
and amomation in clinical biochemistry. Quality control in clinical laboratories. Total
laboratory uncertainty. Accuracy and precision. Selection and optimization of laboratory
methods, Clinical evaluvation of laboratory methods.
Biochemical analysis in urine. Clinical biochemical analysis of proteins. Plasma protein
spectrum during inflammation, paraproteins. Blood gases. Electrolytes and acid – base
balance. Regulation of electrolyte content of body fluids and maintenance of pH
reabsorption of electrolytes. Acidosis & Alkaloids and their determination in clinical
laboratory. .(chalk and talk)
Unit -II
Disorder of carbohydrate metabolism: Diabetes mellitus, classification, etiology,
management, laboratory investigations- GTT. HB Alc. Diabetic complications, sugar levels
in blood, threshold for glucose, factors influencing blood glucose level. Glycogen storage
diseases, pentosuria, and galactosemsia.
Disorder of protein metabplism: Alpha – fectoprotein, Amyloidosis. Cryoglobulinaemia.
Hypo and hyper immunogammaglobulinaemia.
Unit - III
Disorders of lipids: Plasma lipoproteins, cholesterol, triglycerides & phospholipids in
health and disease. Hyperlipidemia, hyperlipoproteinemia.Gauchers disease. Tay – sachs and
Niemann – Pick disease, ketone bodies. Abetalipoproteinemia. Major Cardio vascular
diseases – Atheroschrosis – risk factors, pathogenesis. Laboratory diagnosis of acute
myocardial infraction.
Inborn error of metabolism: Phenylketonuria, alkaptonuria, albinism, tyrosinosis, mape
syrup urine disease. Leish – Nyhan syndrome, sikle cell anemia.Histidinemia. Abnormalities
in Nitrogen Metabolism Uremia., porphyria and factors affecting nitrogen balance. .(
www.med.muni.cz/patfyz/pdf/new/met)
Unit - IV
Disoders of liver kidney: Biochemical indices of hepatobiliary disease. Bile pigments –
formation of bilirubin, urobilinogen bile acids, jaundice – prehapic, hepatic and posthepatic.
Fatty liver, normal and abnormal functions of liver. Liver function tests, diseases of the liver
– hepatitis, cholestasis, cirshosis. Gallstones. Diagnostic Enzymes – Enzymes in health and
diseases. Disoders of kidney: Assessment of renal function – creatine clearance, renal
calculi, uremia and laboratory investigation of kidney disorders, renal function tests.
Unit - V
Circulation disorders: Composition cells, functions of plasma proteins and lipoproteins in
diseases. Disorders of haemoglobin – thalassemia, sickle cell anemia – Microcytic,
normocytic and macrocytic anemias. Endocrine disorders: Pituitary, thyroid, adrenals and
gonads- hypo and hyper secretion of hormones. Disorders – Graves diseases and Addition
diseases. (Blended mode)
Unit VI:
Diagnosis and interpretation: Evaluation and clinical significance of: Blood gases, Various
electrolytes (Na+, K+, HCO3, etc), Urea, Uric acid. Enzymes; Alkaline phosphatase,
Alanine aminotransferase, Aspartate aminotransferase, Lactate dehydrogenase, Creatine
kinase, Amylase, Lipase. Insulin tolerance test; growth hormone stimulation test;
Adrenocorticotropin, congenital adrenal hyperplasia or hirsutism.
Recommended Books:
I. Rodney F. Boyer - (2010). Biochemistry Laboratory: Modern Theory and Techniques,
2thedition, Pearson Prentice Hall.
II. Undurti N. Das - (2011). Molecular Basis of Health and Disease, 1st edition,Springer.
III. Nanda Maheshwari – (2008). Clinical biochemistry, 1st edition, JAYPEE.
IV. MN Chatterjea, Ranashinde – (2012). Textbook of Medical Biochemistry, 8th edition,
JAYPEE.
V. By William J. Marshall, S. K. Bangert – (1995). Clinical Biochemistry: Metabolic and
Clinical Aspects, 1st edition, Churchillivingstone.
VI. Michael Lieberman, Allan D. Marks – (2009). Marks' Basic Medical Biochemistry: A
Clinical Approach, 3rd edition,Lippincott Williams & Wilkins.
VII. Miriam D. Rosenthal, Robert H. Glew – (2009). Medical Biochemistry: Human
Metabolism in Health and Disease, 1st edition, Wiley.
COURSE OUTCOME:
1. An advanced understanding and applied knowledge of the theory and practice of
clinical biochemistry.
2. The student will be able to describe the structure, function and metabolic pathways
for carbohydrates, amino acids and lipids.
3. To learn the alterations in lipid and carbohydrate metabolism that occur as a result of
diabetes.
4. Explain the metabolism of lipoproteins, medical problems associated with abnormal
lipoprotein levels and therapeutic agents used to treat lipid disorders.
5. To make the students biochemistry of membranes including chemical composition
and structure of biological membranes, as well as drug transporters.
6. To impart thorough knowledge about the biochemical basis of various diseases and
disorders.
7. To study various diagnostic and therapeutic methodologies available for diseases and
disorders. Students can apply biochemistry concepts to solve clinical scenarios.
8. Describe intercellular and intracellular signal transductions and explain the molecular
mechanism of drug actions.
BC305 MEMBRANE BIOCHEMISTRY
Objectives:
➢ To understand the biological importance membrane biochemistry.
➢ To study the importance of membrane transport.
Unit-I
Biological membrane: Structure, and assembly: constituents, bacterial cell envelope,
asymmetry flip flop, protein lipid interaction, factors affecting physical properties of
membranes. Membrane models: biological and physical models: energetics and
transduction phenomena, biochemical chemiosmotic hypothesis of Mitchell.(Chalk and
talk)
Unit-II
Physical organization of Membrane Bilayers: Human erythrocyte membrane as a
prototype plasma membrane, role of cytoskeleton in organization of bilayers. Liposomes;
preparation, properties and application in membrane biochemistry. Asymmetry of lipid
distribution in bacterial, plant, and animal membranes, Lateral heterogeneity of membrane
lipids; lipid domains, lipid rafts, Non bilayer lipids and their role in membranes.(Blended
mode of te\ching)
Unit-III
Membrane transport: Diffusion, passive, active and facilitated, transport role of proteins in
the process, exocytosis, receptor mediated endocytosis, osmoregulation. Assembly of virus
membrane receptor.(Flipped mode)
Unit-IV
Specialized mechanism for transport of macromolecules: Na, H dependent processes
and phosphotranferase synthesis, gap junctions, nuclear pores, toxins, control of
transport processes, binding proteins, hormone effects and the role of lipids. Role of Na, K
ATPase and the passive permeability of the plasma membrane to Na, K and Cl,
voltage and ligand gated ion channels, ATP-ADP exchanger.
Unit-V
Mechanistic action of Membrane: Molecular mechanisms, ion translocating antibiotics,
valinomycin, gramicidin, ouabain, group translocation, ionophores, electrical gradient,
energy coupling mechanism. Penetrating the defenses: how antimicrobial agents reach
their targets, cellular permeability barrier to drug penetration, some examples of
modes of penetration of antimicrobial agents, the exploitation of transport systems
in the design of new antimicrobial agents.
UNIT VI:
Membrane asymmetry and its significance in membrane structure and function. Various
techniques to determine asymmetry. Its implications in health and disease. Its role in
membrane signalling.
Reference Books:
1. Membranes and their cellular functions- IB Filnean, R.Coleman and RH Michell, 1984,
Blackwell scientific publishers, Oxford, 3rd ed.
2. Molecular Cell Biology; Lodish et al., 7th Edn. W.H. Freeman and Co. 2012.
3. Introduction to Biological Membranes; William Still well, Elsevier 2013.
4. Biochemistry-G Zubay , Addison Wesley, 1983
5. Biochemistry, L Stryer, 3rd/4th/5th ed, 1989 , Freeman and Co. NY
6. Principles of Biochemistry –Lehninger .
7. Harper’s Illustrated Biochemistry; 27th Edn. Robert K. Murray, Daryl K. Granner, Victor
W.Rodwell , The McGraw6Hill 2006.
COURSE OUTCOME:
1. To understand the signals in proteins and mRNAs that determine their localisation to
different parts of a cell.
2. Students can be observed the mechanisms that target proteins to particular organelles
or ensure they are secreted from the cell .
3. The various types of post-translational covalent modifications of intra-cellular
proteins and how these modifications regulate protein function and stability, with
particular regard to glycosylation, acylation, prenylation and ubiquitination.
4. To understand how calcium signalling can be divided into elemental and global
events and give examples of the processes which are influenced by these events.
5. Students develop presentational skills associated with giving a short oral presentation
on a specific topic.
6. Describe the major mechanisms of cell/cell signaling in humans, including the
hierarchical nature of the neuroendocrine system.
7. Describe the mechanism of action of the major functional groups of signalling
molecules, including polypeptides (growth hormones, insulin, glucagon), steroids,
thyroxine, retinoic acid, amino acid derived signalling molecules, classical
neurotransmitters & eicosanoids.
8. Discuss the molecular events which occur within the cell in response to the major
groups of signalling molecules and the overall physiological outcomes.
BC307 CONCEPTS IN NEUROCHEMISTRY
Objectives:
To introduce basic concepts about the organization, structure, and function of the
human central nervous system; To enable students to apply these fundamental principles
toward understanding nervous system function and dysfunction and toward clinical problem-
solving in relation to disorders that affect the nervous system, with emphasis on the central
nervous system.
PRE-REQUISITE:
Neuroscience is a stand-alone course but it is expected that students have a basic
understanding of human anatomy and physiology and the basic vocabulary of the anatomical
sciences.
Unit-I
CNS Overview: Introduction to the Brain; Overview of brain systems and general principles
of their functional organization: From cortical maps and subcortical loops to the micro-
structure of brain circuits and their interconnections. CNS Organization; CNS Topography;
Neuroembryology. VASCULATURE: Metabolism, Cerebral blood flow, CSF; Blood
Supply; Stroke.( https://www.msdmanuals.com › ... › Biology of the Nervous System)
Unit-II
CELL BIOLOGY OF NEURONS AND GLIA: Nucleus and gene expression and
regulation, Protein synthesis & translational control (including RNAi), Protein sorting &
trafficking (signal peptides, Golgi, secretory and endocytic pathways), Cytoskeleton &
transport (cytoskeleton, actin, microtubules, intermediate filaments, dendritic and axonal
localization/transport, motors and adaptor), Signaling Pathways. Mitochondria, energy
homeostasis and free radicals/energy metabolism in the neuron, Overview of glial cell
biology & myelination (types of glia, morphology and function, myelination in CNS and
PNS).(Blended mode of teaching)
Unit-III
ELECTRICAL PROPERTIES OF NEURONS: Overview of membrane structure &
membrane transport, membrane potential, Ion channels and Ion Channel activity
(electrochemical gradient), Action potentials, Propagation of action potentials along axons,
Modulating action potential, Electrophysiological techniques for studying action potentials
and ion channels.
Unit-IV
SYNAPTIC TRANSMISSION: Overview of synaptic communication/structure of the
synapse, Neural Signaling:- Neruotransmitters; Action potentials:- Resting potential;
Excitatory; Inhibitory; Threshold; Depolarization; Hyperpolarization; Synapse: Formation;
Synaptic communication; Neural circuits, synaptic plasticity: LTP/LTD, Spike Time
dependent plasticity. Mechanism of neurotransmitter release, postsynaptic response:
electronic properties of dendrites, basic integration, Ionotropic (v) metabotrobic receptors,
Neurochemical transmission: Glutamate, GABA, Glycine, Acetylcholine (Synthesis,
storage, release and inactivation), Dopamine, Norepinephrine, epinephrine, serotonin,
histamine, Neuropeptides & atypical neurotransmitters, Electrical synapses (gap junctions).
Unit-V
DEVELOPMENT & PLASTICITY: Overview of nervous system development/
comparative embryology, Neural induction, Regionalization, Neurogenesis & migration,
Mechanisms of axon guidance & target cell recognition, Synapse formation & elimination,
Neuronal Death.(Chalk and talk)
Unit-VI
TRUAMA AND DISEASE: Development disorders; Degenerative disorders; Psychiatric
disorders; Injury disorders; Others like Epilepsy; Visual Pathways; Occular Movements;
Vascular syndromes; Sensory and Motor Syndromes.
TEXTBOOK
1. J. W. Baynes, M. H. Dominiczak, Medical Biochemistry, 2nd ed., Elsevier Mosby,
Philadelphia, New York, Toronto, 2005.
2. G. Siegel, R.W. Albess, S. Brady, D. Price, Basic Neurochemistry, 7th Edition,
Amsterdam. Tokio, 2006.
3. George J Siegel, MD, Editor-in-Chief, Bernard W Agranoff, MD, R Wayne Albers,
PhD, Stephen K Fisher, PhD, and Michael D Uhler, PhD. Basic Neurochemistry, 6th
edition Philadelphia: Lippincott-Raven; 1999.
4. Dale purves , George j. Augustine, David fitzpatrick , William c. Hall, Anthony-
samuel lamantia , James o. Mcnamara , S. Mark williams. Neuroscienc ethird edition
Publishers Sunderland, Massachusetts U.S.A, 2004.
5. Siegel, George and R. Wayne Albers, Scott Brady and Donald Price Basic
Neurochemistry, 7th edition: Molecular, Cellular and Medical Aspects Academic
Press/2005.
6. Haines, Duane Neuroanatomy - An Atlas of Structures, Sections and Systems, 5th
edition Lippincott Williams and Wilkins/2000.
REFERENCE BOOKS
1. Afifi and Bergman, Functional Neuroanatomy, Text and Atlas, McGrawHill, 2nd
Edition, 2005.
2. Haines, Neuroanatomy: An Atlas of Structures, Sections and Systems, 7th ed. Ed.
Lippincott William and Wilkins, 2007.
3. Blumenfeld, Neuroanatomy Through Clinical Cases (Paperback), Sinauer
Associates; 2nd edition (2010).
COURSE OUTCOME:
1. Neurochemistry is the scientific study of the chemical interactions of the
brain and nervous system.
2. Ultimate goal is to understand higher brain function at a variety of levels.
3. Understand the properties of cells that make up the nervous system including
the propagation of electrical signals used for cellular communication.
4. Relate the properties of individual cells to their function in organized neural
circuits and systems.
5. Understand how the interaction of cells and neural circuits leads to higher
level activities such as cognition and behaviour.
6. An understanding of the influence of family, community, and society in the
care of people with neurological disorder.
i. Evaluate and discuss primary research literature and evaluate the validity of
hypotheses generated by others.
7. This course is providing you with the requisite skills to effectively
communicate scientific and medical information to diverse audiences.
8. Understanding pathophysiology, work-up, and treatments for Disease
Specific Knowledge.
ED Papers
BC3ED - DEVELOPMENTAL BIOLOGY (ED PAPER)
Objectives
i. To understand the molecular and cellular mechanisms of development and learn
about basic embryology
ii. To understanding the students will be able to generally describe the concepts of
cellular competence, induction, specification, commitment and differentiation in
embryonic development.
iii. To recognize the how to explain at least two concepts in developmental biology that
overlap with other sciences, such as stem cell research, cancer research, evolutionary
sciences, or neuroscience.
iv. Students will be able to discern and summarize the current state of knowledge on a
given topic, construct pioneering research questions on that topic, and propose
experiments aimed at answering those questions.
v. To make the students how the knowledge in genetics, evolutionary biology, cell
biology, developmental biology, physiology and ecology.
Unit - I
Emergence of evolutionary thoughts: Lamarks; Darwin – concepts of variation, adaptation,
struggle, fitness and natural selection; Mendelism; spontancity of mutations; the
evolutionary synthesis, Origin of cells and unicellular evolution; Origin of basic biological
molecules; abiotic synthesis of organic monomers and polymers; concept of Oparin and
Haldane; experiment of Miller (1953); the first cell; evolution of prokaryotes; origin of
eukaryotic cells; evolution of unicellular eukaryotes; anaerobic metabolism, photosynthesis
and aerobic metabolism.(Blended mode of teaching)
Unit - II
Basic concepts of development: Potency, commitment, specification, induction, competence,
determination and differentiation; morphogenetic gradients; cell fate and cell lineages; stem
cells; genomic equivalence and the cytoplasmic determinants; imprinting; mutants and
transgenics in analysis of development.(cmlearn.unito.it/mod/book/tool)
Unit -III
Gametogenesis, Fertilization and early development: Production of gametes, cell surface
molecules in sperm-egg recognition in animals; embryo sac development and double
fertilization in plants; zygote formation, cleavage, blastula formation,embryonic fields,
gastrulation and formation of germ layers in animals; embryogenesis, establishment of
symmetry in plants; seed formation and germination.
Unit - IV
Morphogenesis and organogenesis in animals: Cell aggregation and differentiation in
Dictyostelium; axes and pattern formation in Drosophila, organogenesis – vulva formation
in Caenorhabditiselagans; eye lense induction, limb development and regeneration in
vertebrates; differentiation of neurons, post embryonic development- larval formation,
metamorphosis; environmental regulation of normal development; sex determination.
Unit - V
Morphogenesis and organogenesis in plants: Organization of shoot and root apical meristem;
shoot and root development; lead development and phyllotaxy; transition to flowering, floral
development in Arabidopsis and Antirrhunu.(https://academic.oup.com/botlinnean/article-
pdf/.).
Unit VI:
Medical implications of developmental biology-genetic errors/ teratogenesis/ stem cell
therapy.
Recommended Books:
5. Principles of Development. 3rd edition, by L. Wolpert, 2006, Oxford University
press, incorporated.
6. Developmental Biology. 3rd edition, by Lewis Wolpert, 2006, Oxford University
Press, USA
7. Developmental Biology, 6th edition by Scott Gillbert, 2000, Sunderland
(MA): Sinauer Associates; ISBN-10: 0-87893-243-7
8. Evolutionary developmental biology, 2nd edition by Brain K. Hall. 1998,
Springer;ISBN-10: 0412785803
COURSE OUTCOME:
9. To Understand the molecular and cellular mechanisms of development and
learn about basic embryology
10. To understanding the students will be able to generally describe the concepts
of cellular competence, induction, specification, commitment and
differentiation in embryonic development.
11. To understand the how to explain at least two concepts in developmental
biology that overlap with other sciences, such as stem cell research, cancer
research, evolutionary sciences, or neuroscience.
12. Students will be able to discern and summarize the current state of knowledge
on a given topic, construct pioneering research questions on that topic, and
propose experiments aimed at answering those questions.
13. To make the students how to understand the knowledge in genetics,
evolutionary biology, cell biology, developmental biology, physiology and
ecology.
14. It is useful for awareness of scientific methods and research skills used to
investigate cell & developmental biology problems
15. To awareness of ethical issues in cell and developmental biology research,
particularly in relation to stem cells, in vitro fertilisation and assisted
reproductive technologies.
16. Students can understand the capacity to evaluate and synthesise information
from a wide range of sources in order to communicate ideas, concepts and
construct arguments in both non-scientific and scientific language.
BC2ED - GENETICS (ED PAPER)
Objectives
i. Identify and describe the process and purposes of the cell cycle, meiosis, and mitosis,
as well as predict the outcomes of these processes.
ii. Transmission genetics problems, make accurate predictions about inheritance of
genetic traits, and map the locations of genes
iii. To identify the parts, structure, and dimensions of DNA molecules, RNA molecules,
and chromosomes, and be able to categorize DNA as well as describe how DNA
is stored
iv. To describe what causes and consequences of DNA sequence changes and how cells
prevent these changes, as well as make predictions about the causes and effects
of changes in DNA
v. To describe applications and techniques of modern genetic technology, as well as
select the correct techniques to solve practical genetic problems
Unit - I
Introduction to Genetics: Brief history/basic concepts of genetics, Cell division and
chromosomes. Mendelian genetics/monohybrid, dihybrid cross. Mendelian
genetics/trihybrid cross, probability. Modification of Mendelian ratios/incomplete and
codominance.Modification of Mendelian ratios/incomplete and codominance.Structure of
Gene - Interaction of Gene - Commentary Factors, Supplementary Factors, Inhibitory and
Lethal Factors - Atavism. . (https://www.slideshare.net/vanessaceline/intorduction-to-
genetics)
Unit - II
Diploid chromosomes number.Sex differentiation and sex determination.The X
chromosomes, Barr bodies, the Lyon hypothesis. Aneuploidy and polyploidy: Gene deletion,
duplication, inversions and translocation. Sex Linkage in Drosopohila and Man, Sex
Influenced and Sex Limited Genes - Non-Disjunction and Gynandromorphs - Cytoplasmic
Inheritance - Maternal Effect OnLimnaea (Shell Coiling), Male Sterility (Rode's
Experiment).CO2 sensitivity In Drosophila, Kappa particles in Paramecium, Milk Factor in
Mice.(Blended mode )
Unit - III
Blood Groups and their Inheritance in Human - Linkage and Crossing Over:- Drosophila -
Morgans' Experiments - Complete and Incomplete Linkage, Linkage Groups, Crossing Over
types, Mechanisms - Cytological Evidence for Crossing Over, Mapping of Chromosomes -
Interference and Coincidence.
Unit -IV
Nature and Function of Genetic Material - Fine Structure of the Gene - Cistron, Recon,
Muton - Mutation - Molecular Basis of Mutation, Types of Mutation, Mutagens, Mutable
and Mutator Genes. Chromosomal Aberrations - Numerical and Structural Examples from
Human.
Unit -V
Applied Genetics - Animal Breeding - Heterosis, Inbreeding, Out Breeding, Out Crossing,
Hybrid Vigour. Population Genetics, Evolutionary genetics, Hardy Weinberg Law - Gene
Frequency, Factors Affecting Gene Frequency, Eugenics, Euphenics and Euthenics,
Bioethics. www.goldiesroom.org/...)
Unit VI:
Genetic Principles and their application in medical practice; Case studies (Interacting with
patients, learning family history and drawing pedigree chart); Syndromes and disorders:
definition and their genetic basis - Cystic fibrosis and Tay Sach’s Syndrome;
Phenylketonuria and Galactosemia; Ethical issues with clinical genetics.
Recommended Books:
1. Genetics by Verma, P.S. and V. K.Aggarwal.
2. Genetics by Russell P.J.
3. Genetics analysis and principles by Brooker R.J and McGraw Hill.
4. Basic Genetics my Miglani G.S.
5. Genetics: Analysis of genes and genomes by Hartl D.L and Jones E.W.
COURSE OUTCOME:
1.Identify and describe the process and purposes of the cell cycle, meiosis, and
mitosis, as well as predict the outcomes of these processes.
2.Transmission genetics problems, make accurate predictions about inheritance of
genetic traits, and map the locations of genes.
3.To identify the parts, structure, and dimensions of DNA molecules, RNA
molecules, and chromosomes, and be able to categorize DNA as well as describe how DNA
is stored.
4.To describe what causes and consequences of DNA sequence changes and how
cells prevent these changes, as well as make predictions about the causes and effects of
changes in DNA.
5.To describe applications and techniques of modern genetic technology, as well as
select the correct techniques to solve practical genetic problems.
6.To carry out genetics laboratory and field research techniques.
7.To describe experimental results in written format both informally and in formal
manuscript format.
8.To accurately diagram and describe the processes of replication, transcription,
translation, as well as predict the outcomes of these processes"
BC3ED-1 COMPUTATIONAL BIOLOGY
Objective:
The main objective of this course is to provide foundation in fundamental concepts,
tools and resources in Computational Biology. A sound foundation in Mathematics
algorithms and Statistics is essential for analysis of biological data. It is necessary to develop
programming skills in languages like C++, PERL, Python and Java.
Unit-I Biochemistry and Biophysics: Laws of chemistry and physics, quantum mechanics,
Structure of atom, molecular orbitals and covalent bonds, molecular interactions,
Steriochemistry, Structure of Protein, DNA and RNA (primary/secondary/tertiary structure;
atoms, bonds, backbones, torsion angles), Amino and Nucleic Acids (hydrophobicity,
polarity, charge, aromatic rings), Force Fields (charge, radii, electrostatics, van der Waals,
stacking, hydrogen bonds), Structure Determination (Crystallography, NMR), Structure
Modeling (Folding, docking, dynamics, mutagenesis effects).(Blended of teaching)
Unit-II Applied mathematics: Numerical descriptive techniques: Measures of central
tendency, Correlation and Regression, Matrices and Linear Algebra, Vector Analysis,
Trigonometry and Analytical Geometry, Calculus, Numerical Methods.(Problem based
learning)
Unit-III Algorithms: Algorithms in Computing, Algorithm design techniques, Greedy
Algorithms, Dynamic Programming Algorithms, Divide-and-Conquer Algorithms,
Combinatorial Pattern Matching, Expectation and Maximation, Genetic Algorithm Hidden
Markov Models, Clustering and Trees.
Unit-IV Computing: Programming languages, Algorithm, Flowchart, Compiling, Testing
and Debugging, Documentation – Data structures – Array, Stack, Queue, Linked List
concepts, Programming in C and C++, Perl & Bioperl, Java Basics.
Unit-V Modeling tools and resources: Protein Databases: BLAST/NCBI, Protein Data
Bank, SCOP, OrthoMCL, • Structure: PyMol, ConSurf, Modeller, TMalign, DALI, DSSP,
Macromolecular Docking/Interfaces: ZDOCK, PatchDock, KFC2, Molecular Dynamics:
OpenMM (CHARMM, AMBER, GROMACS FFs), Electrostatics: PDB2PQR, APBS.
Unit VI:
Information search and data retrieval Introduction, tools for web search, data
retrieval tools, data mining of biological databases, biological databases, difference between
primary, secondary and tertiary databases, types of databases. Probabilistic information
retrieval, language models for information retrieval, managing bioinformatics tools,
command line sequence extraction and analysis.(Student led learning)
Text Book:
1. Biostatistics (9th Ed.) by Wayne W. Daniel. John Wiley. 2004
2. Programming in ANSI C (4th Ed.) by E. Balagurusamy. Tata McGrawHill
Publishing Company Limited. 2007
3. Algebra (3rd Ed.) by Serge A. Lang. Pearson education. 2003
4. Introduction to Calculus & Analysis, Vol I and II by Richard Courant & Fritz John,
Springer publisher.1999.
5. An introduction to bioinformatics algorithms by Neil C. Jones, Pavel Pevzner. MIT
Press. 2004
Reference book:
1. Statistical Methods by N. G. Das, Vol: I and II. The McGraw-Hill Companies. 2009
2. Beginning PERL for Bioinformatics by James Tisdall. O’Reilly publications.2001
3. Basic mathematics by Serge A. Lang, Springer publisher. 1988.
COURSE OUTCOME:
1. Explain the origin, rationale and uses of large datasets used to study biological
processes in living organisms.
2. Perform computational analyses of biological datasets and relate the results to core
principles in biology.
3. Use computational methods to help execute a biological research plan.
4. Analyse biological problems from global and ethical impact perspectives (impact of
computational biology methods).
5. Students will also appreciate diverse applications in machine learning, robotics,
communications, biology, ecology, brain science, sociology, and economics.
6. The course will emphasize the fundamental underpinnings of network science to
graph-theoretic concepts and graph algorithms and so will focus on algorithmic,
computational, and statistical methods of network science.
7. The course will go beyond the strictly structural concepts of small-world and scale-
free networks, focusing on dynamic network processes such as epidemics,
synchronization, or adaptive network formation.
8. The program provides the student with a broad scientific foundation
suitable immediately upon graduation for careers in biological information analysis
in fields like: bioinformatics, the biotechnology industry, medicine, research in
computational biology or bioinformatics, healthcare, or the chemical and molecular
disciplines.