chemical composition of the body
TRANSCRIPT
Chapter 2
Chemical Composition of the Body
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Objectives
Explain how covalent bonds are formed and distinguish between nonpolar and polar covalent bonds.
Describe the nature of hydrogen bonds and explain their significance.
Describe the structure of DNA and RNA, and explain the law of complementary base pairing.
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Chemical Bonds, Molecules, and Ionic Compounds
Chemical bonds: Interaction of valence electrons
between 2 or more atoms. Number of bonds determined by
number of electrons needed to complete outermost shell.
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Covalent Bonds
Atoms share their valence electrons.
Nonpolar covalent bonds:
Electrons are equally distributed between the two identical atoms.
Strongest bond. H2 and 02.
Figure 2.2
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Covalent Bonds (continued)
Polar bonds: Electrons are
shared between two different atoms.
Electrons may be pulled more toward one atom.
Has + and – poles. Oxygen, nitrogen,
phosphorous have tendency to pull electrons towards themselves.
Figure 2.4
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Ionic Bonds
One or more valence electrons from one atom are completely transferred to a second atom.
Cation and anion attract, form ionic compound.
Weaker than polar covalent bonds.
Dissociate easily when dissolved in H20.
Form hydration spheres.
Make an ion/molecule more soluble.
NaCl Na++ Cl-
Figure 2.6
Figure 2.5
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Ionic Bonds (continued)
Glucose, amino acids, are H20 soluble. Hydration spheres form around atoms of
oxygen, nitrogen, phosphorous. Hydrophilic molecules.
Molecules composed of nonpolar covalent bonds are not H20 soluble. Cannot form hydration spheres.
Hydrophobic molecules.
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Hydrogen Bond
Hydrogen forms a polar bond with another atom, giving hydrogen has a slight + charge.
Weak attraction for a second electronegative atom.
Surface tension.
Insert fig. 2.7
Figure 2.7
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Acid/Base
Acid: Molecule that can release protons
(H+). Proton donor.
Base: Negatively charged ion that can
combine with H+, and remove it from solution.
Proton acceptor.
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pH
pH = log _1__ [H+] [H+] = molar concentration of H+. pH inversely related to [H+].
Because of logarithmic relationship, a solution with 10 times [H+] of H20 has a pH = 6; solution with 0.1 the [H+] has a pH = 8.
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Organic MACROMolecules
Molecules that contain carbon and hydrogen.
Carbon has 4 electrons in outer shell and covalently bonds to fill its outer shell.
Functional groups: Inactive “backbone” to
which more reactive atoms are attached.
Carbonyl group: Aldehydes and ketones.
Carboxyl group: Organic acids (lactic and
acetic acids). Hydroxyl group:
Alcohol. Figure 2.10
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Carbohydrates Organic molecules that
contain carbon, hydrogen and oxygen.
CnH2n0n. Monosaccharides:
Simple sugars. Glucose, fructose, galactose.
Disaccharide: 2 monosaccharides joined
covalently. Sucrose (glucose and
fructose), lactose (glucose and galactose), maltose (2 glucose).
Polysaccharide: Numerous monosaccharides
joined covalently. Starch (thousands of glucose
joined), glycogen (repeating glucose joined that are highly branched).
Mechanism for storing energy with less osmotic H20 movement.
Figure 2.13
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Lipids
Diverse group of molecules. Differ greatly in chemical structure. Insoluble in polar solvents (H20). Consist primarily of hydrocarbon chains
and rings. Hydrophobic.
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LIPIDS: Triglycerides (triacylglycerol)
Formed by condensation of glycerol and 3 fatty acids.
Fatty acids consist of nonpolar hydrocarbon chain with carboxyl end.
Saturated: Hydrocarbon chains
joined by single covalent bonds.
Unsaturated: Double covalent bonds
within hydrocarbon chain.
Figure 2.17
Figure 2.18
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LIPIDS:Ketone Bodies
Hydrolysis of triglycerides in adipose tissue release free fatty acids.
Free fatty acids can be converted in the liver to ketone bodies.
Ketoacidosis: Increased ketone
bodies in the blood which lowers pH.
Figure 2.19
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LIPIDS: Phospholipids
Phospholipids: Number of different
categories of lipids that contain phosphate group.
Nonpolar end is hydrophobic, polar end is hydrophilic.
Lecithin: Phosphate attached to
a nitrogen-containing choline molecule.
Figure 2.20
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LIPIDS: Steroids
All have same basic structure; three 6-carbon rings joined to a 5-carbon ring. Nonpolar and
insoluble in H20. Cholesterol is
precursor for steroid hormones.
Figure 2.22
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LIPIDS: Prostaglandins
Fatty acid with cyclic hydrocarbon group.
Derived from arachidonic acid.
Serve a variety of regulatory functions.
Blood vessel diameter, ovulation, uterine contractions, inflammation, blood clotting.
Figure 2.23
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Proteins Large molecules
composed of long chains of amino acids.
20 different amino acids can be used in constructing a given protein.
Each amino acid contains an amino group (NH2) at one end and carboxyl group (COOH) at the other end.
Differences between amino acids are due to differences in functional groups (“R”).
Figure 2.24
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Protein Structure Level
Primary structure: Sequence of the amino acids
in the protein is described. Secondary structure:
Weak hydrogen bonds form between hydrogen of 1 amino acid and the and oxygen of a different amino acid nearby.
a-helix or b-sheet. Tertiary structure:
Polypeptide chains bend and fold to produce 3 -dimensional shape.
Formed and stabilized by weak chemical bonds between functional groups.
Quaternary structure: Number of polypeptide
chains covalently linked together.
Figure 2.26
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Nucleic Acids
Include DNA and RNA. Nucleotides:
Subunits of nucleic acids bonded together to form long polynucleotide chains.
Each composed of 3 smaller units:
5-carbon sugar. Phosphate group
attached to one end of sugar.
Nitrogenous base attached to other end of sugar.
Nitrogenous bases: Pyrimidines: single ring
of carbon and nitrogen. Purines: two rings of
carbon and nitrogen.Figure 2.29
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NUCLEIC ACIDS: DNA and RNA
DNA: Basis of genetic code. Deoxyribose covalently
bonded to 1 of 4 bases: Purines: guanine and
adenine. Pyrimidines: cytosine and
thymine. Sugar-phosphate bonds
form the chain. Each base can form
hydrogen bonds with other bases.
Two strands are are produced by hydrogen bonding.
RNA: Consists of a single long
chain of nucleotides joined together by sugar-phosphate bonds.
Ribose covalently bonds to 4 bases.
Uracil replaces thymine.
Figure 2.32