the structure and function of macromolecules · 2018. 9. 6. · macromolecules are polymers...
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The Structure and Function of Macromolecules
Macromolecules are polymers
• Polymer – long molecule consisting of many similar building blocks.
• Monomer – the small building block molecules.
• Carbohydrates, proteins and nucleic acids are polymers.
• There are 1000’s of different kinds of macromolecules, and an enormous variety of polymers can be built from a small set of monomers.
Fig. 5-2
Short polymer
HO 1 2 3 H HO H
Unlinked monomer
Dehydration removes a water molecule, forming a new bond
HO
H2O
H 1 2 3 4
Longer polymer
(a) Dehydration reaction in the synthesis of a polymer
HO 1 2 3 4 H
H2O Hydrolysis adds a water molecule, breaking a bond
HO H H HO 1 2 3
(b) Hydrolysis of a polymer
Carbohydrates
• Function – fuel and building material.
• Simplest carbohydrate – monosaccharides (single sugars) – are the monomers of polysaccharides.
• Monosaccharides usually have molecular formulas (CH2O)n the most common monosaccharide, glucose is C6H12O6
Monosaccharides
• Can be drawn as linear skeletons, but many sugars form rings in aqueous solutions.
• Note the abbreviated form, and numbering.
Disaccharides
• Disaccharides are formed when dehydration reaction joins two monosaccharides.
• Glycosidic linkage – the covalent bond that forms between the monosaccharides.
• Note the linkage between two glucose molecules to form maltose, and the linkage to form sucrose from glucose and fructose is specified by which carbons of the ring are joined.
Fig. 5-5
(b) Dehydration reaction in the synthesis of sucrose
Glucose Fructose Sucrose
Maltose Glucose Glucose
(a) Dehydration reaction in the synthesis of maltose
1–4 glycosidic
linkage
1–2 glycosidic
linkage
Polysaccharides
• Polymers of sugar – have storage and structural roles.
• Starch – storage polysaccharide of plants – Monomer: glucose
Amylose – unbranched form, Amylopectin – branched form
Glycogen
• Storage polysaccharide in animals – in humans glycogen is mainly found in liver and muscle cells.
Note the more extensive branching , means more ends of chains where single glucose molecules can be broken off for energy – available rapidly.
Cellulose
• Structural polysaccharide – component of the cell wall of plants.
• Polymer of glucose, but the glycosidic linkages differ.
– Two ring forms of glucose alpha () and beta (β) are responsible for the difference.
Glucose β Glucose
Fig. 5-7bc
(b) Starch: 1–4 linkage of glucose monomers
(c) Cellulose: 1–4 linkage of glucose monomers
β
Cellulose
• Polymers with glucose are helical
• Polymers with β glucose are straight – In the straight chains, H atoms on one strand can
bond with OH groups on other strands.
• The cellulose molecules grouped together form strong building materials for plants.
• As well, the enzymes that carry out hydrolysis of glycosidic linkages can’t hydrolyze β glycosidic linkages.
Cellulose
• Cellulose in the human diet passes through the digestive tract.
• Even though no energy is extracted, insoluble fibre is still important to healthy functioning of the digestive tract.
• The only organisms capable of breaking down cellulose are microbes, and those organisms like cows, and termites that have those microbes living in their digestive tracts.
Lipids
• Do not form polymers, instead have a unifying characteristic:
– Little or no affinity for water (non-polar).
– Hydrophobic because they consist mainly of hydrocarbons.
Fats
• Fats are made from two smaller molecules: glycerol and fatty acids.
Fatty acid Glycerol Dehydration reaction in the synthesis of a fat
Fig. 5-11b
(b)
Fat molecule (triacylglycerol)
Ester linkage
Fats
• Fats separate from water because water molecules form hydrogen bonds with each other, and exclude the fats.
• In a fat, three fatty acids are joined to glycerol by an ester linkage, creating a tryacylglycerol, or triglyceride.
Fatty acids
• Fatty acids vary in length (# of C’s) and number and location of double bonds.
• Saturated fatty acids – maximum number of hydrogen atoms possible, no double bonds
• Unsaturated fatty acids – one or more double bonds, fewer hydrogens
– Monousaturated – one double bonds
– Polyunsaturated – two or more double bonds
Fats
• Fats made from saturated fatty acids are solid at room temp.
• Most animal fats are saturated.
• Fats made from unsaturated fatty acids are liquid at room temp. - oils.
• Plants fats are usually unsaturated.
Fats and diet
• A diet rich in saturated fats may contribute to atherosclerosis – plaque deposits lining the arteries leading to cardiovascular disease.
• Trans fats – formed by hydrogenation which adds hydrogen to unsaturated fats.
• These fats may contribute more that saturated fats to cardiovascular disease.
Function
• Major function of fats – energy storage.
• In humans fat is stored in adipose cells – very compact, very little water.
• Fats also have 2X the energy per gram of carbohydrate
• Fats also function in insulating the body, and cushioning vital organs
Phospholipid
• In a phospholipid, two fatty acids attach to glycerol, along with a phosphate group.
• The two fatty acid tails are hydrophobic, but the phosphate group forms a hydrophilic head.
• When phospholipids are added to water, they self assemble with the hydrophobic tails pointing to the interior.
Fig. 5-13
(b)
Space-filling model (a)
(c)
Structural formula Phospholipid symbol
Fatty acids
Hydrophilic head
Hydrophobic tails
Choline
Phosphate
Glycerol
Hyd
rop
ho
bic
tai
ls
Hyd
rop
hili
c h
ead
• Phospholipids are assembled into a bilayer with tails away from water, that is the major component of cell membranes.
Steroids
• Steroids all have a carbon skeleton consisting of four fused rings.
• Cholesterol – component of animal cell membranes, also precursor to forming steroid hormones such as estrogen and testosterone.
Proteins
• Proteins have diverse structure meaning they have a wide range of functions.
– As catalysts called enzymes speeding up the rate of reaction in organisms , can be used repeatedly as they are not used up in the reaction
– Structural support, cellular communications, movement, defense against foreign substances
Amino acids
• Amino acids have a central carbon that has a carboxyl group, an amino group, a hydrogen and an R group attached.
• Amino acids differ in their properties based on different R groups or side chains.
Fig. 5-UN1
Amino group
Carboxyl group
carbon
Fig. 5-17a
Nonpolar
Glycine (Gly or G)
Alanine (Ala or A)
Valine (Val or V)
Leucine (Leu or L)
Isoleucine (Ile or I)
Methionine (Met or M)
Phenylalanine (Phe or F)
Tryptophan (Trp or W)
Proline (Pro or P)
Fig. 5-17b
Polar
Asparagine (Asn or N)
Glutamine (Gln or Q)
Serine (Ser or S)
Threonine (Thr or T)
Cysteine (Cys or C)
Tyrosine (Tyr or Y)
Fig. 5-17c
Acidic
Arginine (Arg or R)
Histidine (His or H)
Aspartic acid (Asp or D)
Glutamic acid (Glu or E)
Lysine (Lys or K)
Basic
Electrically charged
Polypeptides
• Polypeptides are polymers built from their monomer, amino acids.
• Peptide bond – covalent bond between the carboxyl group of one amino acid and the amino group of the next amino acid.
• Polypeptides range in length up to thousands of monomers.
• Each polypeptide has a unique sequence of amino acids.
• A protein is made of one or more polypeptides in a unique three dimensional shape.
Peptide bond
Fig. 5-18
Amino end (N-terminus)
Peptide bond
Side chains
Backbone
Carboxyl end (C-terminus)
(a)
(b)
Fig. 5-19
A ribbon model of lysozyme (a) (b) A space-filling model of lysozyme
Groove
Groove
A functional protein consists of one or more polypeptides twisted, folded, and coiled into a unique shape
STRUCTURE dictates FUNCTION
• The sequence of amino acids determines a protein’s 3D structure
• A protein’s structure determines its function
Levels of Structure
• Primary structure – unique sequence of amino acids
• Secondary structure – coils and folds in the polypeptide chain
• Tertiary structure – determined by interactions between side chains.
• Quaternary structure – a protein that consists of multiple polypeptide chains.
Fig. 5-21a
Amino acid subunits
+H3N Amino end
25
20
15
10
5
1
Primary Structure
The sequence of amino acids is like the order of letters in a long word.
Primary structure is determined by inherited genetic information.
Primary structure
• A slight change in primary structure can affect a protein’s ability to function if it affects its shape.
• Example:
– Sickle-cell – inherited blood disorder caused by a single amino acid change in the protein hemoglobin
Fig. 5-22
Primary structure
Secondary and tertiary structures
Quaternary structure
Normal hemoglobin (top view)
Primary structure
Secondary and tertiary structures
Quaternary structure
Function Function
subunit
Molecules do not associate with one another; each carries oxygen.
Red blood cell shape
Normal red blood cells are full of individual hemoglobin moledules, each carrying oxygen.
10 µm
Normal hemoglobin
1 2 3 4 5 6 7
Val His Leu Thr Pro Glu Glu
Red blood cell shape
subunit
Exposed hydrophobic region
Sickle-cell hemoglobin
Molecules interact with one another and crystallize into a fiber; capacity to carry oxygen is greatly reduced.
Fibers of abnormal hemoglobin deform red blood cell into sickle shape.
10 µm
Sickle-cell hemoglobin
Glu Pro Thr Leu His Val Val
1 2 3 4 5 6 7
Fig. 5-22c
Normal red blood cells are full of individual hemoglobin molecules, each carrying oxygen.
Fibers of abnormal hemoglobin deform red blood cell into sickle shape.
10 µm 10 µm
Secondary structure
• helix – coiled regions
• β pleated sheet - folded sections
• The coils and folds of secondary structure result from hydrogen bonds between repeating parts of the polypeptide backbone.
Fig. 5-21c
Secondary Structure
pleated sheet
Examples of amino acid subunits
helix
Tertiary Structure
• Interactions among side chains including:
– Hydrogen bonds,
– Hydrophobic interactions
– Strong covalent bonds called disulfide bridges
Quaternary Structure
• When two or more polypeptide chains form one macromolecule
• Examples:
– Collagen consists of three polypeptides
– Hemoglobin consists of four polypeptides (2 alpha and 2 beta chains)
Fig. 5-21g
Polypeptide chain
Chains
Heme
Iron
Chains
Collagen
Hemoglobin
Determining Protein Structure
• Physical and chemical conditions can affect the structure of proteins.
• Alterations in pH, salt concentration, and temperature can cause a protein to unravel.
• Denaturation – the loss of a protein’s proper 3D structure.
• A denatured protein is unable to function.
Folding assistance
• Chaperonins – proteins that assist in the proper folding of other polypeptides
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