Outline: Amino acids Polymerisation of Amino Acids Protein Structures Classification of Proteins Properties of Proteins

Organic macromolecules in living organisms. Composed of one or more polypeptide chains. Polymers from condensation of many basic units of amino acids joined by peptide bonds. Elements : C, H, O, N, S, P

Proteins are polymers of amino acids Each amino acid has a central carbon atom (the alpha carbon) to which are attached a hydrogen atom, an amino group NH2, A carboxylic acid group COOH, and one of 20 different types of R groups 20 different amino acids that make up proteins. Each amino acid is different from the other by having different R-side chains /groups. Four main classes depending on R-side chains : nonpolar, polar, acidic and basic groups.

amino group

R group

carboxyl group

One group of amino acids has hydrophobic R groups.

 Another group of amino acids has polar R groups hydrophilic

The last group of amino acids with functional groups that are charged (ionized) at cellular pH. Some R groups are bases, others are acids.

Amino acids joined together end-to-end

COOH of one amino acid (AA) covalently bonds to the NH2 of the next AA Special name for this bond - Peptide Bond
Two AAs bonded together Dipeptide Three AAs bonded together Tripeptide Many AAs bonded together Polypeptide

Characteristics of a protein determined by composition and sequence of AAs Virtually unlimited number of proteins

Two amino acids

1. Colloid solution of large molecules. 2. Amphoteric with both positive and negative charges due to side chains of component amino acids. 3. At isoelectric point, proteins are least soluble due to intermolecular bonding of positive and negative charges. 4. Buffer protein molecules can resist pH changes due to side chains that bind with H+ or OH- ions.

12

1) Primary structure:

The specific linear sequence of amino acids The way the amino acid chain coils or folds Coils to form right-handed -helix, held together by hydrogen bonds between every 4th amino acid. E.g fibrous protein: keratin in hair, nails, horn & feathers Folds to form -pleated sheets. Polypeptide chains lie parallel to one another & are held together by hydrogen bonds & folded longitudinally. High resistance to stretching. E.g. silk protein fibroin

2) Secondary structure:

14

15

3) Tertiary structure : Formed by folding & coiling of the secondary structure of polypeptide chains to form a three-dimensional shape of a precise & compact globular protein Hydrogen bonds, ionic bonds, disulphide bonds, hydrophobic interactions & Van der Waals interactions. E.g. enzyme, antibodies, plasma protein, hormones and myoglobin.

17

4) Quaternary structure: Consists of two or more polypeptide chains which are held together by hydrogen bonds, ionic bonds and hydrophobic interactions. E.g. haemoglobin contains 4 globular polypeptide chains, two and two - polypeptide chains each containing an iron & containing haem group.

19

20

 Structure fibrous, globular & intermediate proteins Composition simple & conjugated proteins Functions structure, catalysis, signals, movement, defense & storage

21

Fibrous proteins Eg. Collagen, keratin, fibrin & myosin Form body structures of animals Globular proteins Eg. Globulin, enzymes, antibodies , hormones

Intermediate proteins Eg. Fibrinogen, a plasma protein used for blood clotting

Secondary structure Insoluble in water Helical structures or pleated sheets held together by hydrogen bonds A stable protein structure Tertiary structures Tightly coiled & folded to form sphere Structure maintained by various bonds Easily soluble in water A fibrous protein but soluble in water

23

Simple proteins Eg. Fibrous protens, globular proteins

Pure proteins, only amino acids and no other substances

Conjugated protein

a complex compound made up of a globular protein tightly bound to a non-protein component known as the prosthetic group. Can be divided into several types depending on the types of prosthetic groups.

Conjugated protein Lipoprotein Glycoprotein (mucin) Chromoprotein

Prosthetic group Lipid

Where it can be found

Component of cell membrane

Metalloprotein

Carbohydr Mucus of respiratory & ate digestive tracts, antibodies, cell membrane Pigment In haemoglobin & myoglobin molecule (the haem group is the pigment molecule) Metal ion In haemoglobin, myoglobin & cytochromes (the haem groups contain Fe2+ ion) Nuclei acid Chromosomes and ribosomes

Nucleoprotein

Type of protein Function Enzymatic Nutrition protein (catalyses the hydrolysis of complex food substances Transport Transport of protein respiratory gases Transport of ions or molecules across cell membrane Contractile protein Movement

Example Digestive enzymes such as carbohydrase, protease & lipase

Haemoglobin
Membrane transport protein

Actin and myosin

Type of protein Function Example Homeostasis Maintenance of Serum albmi protein osmotic pressure in body fluids Hormonal Coordination Non-steroid protein hormones such as insulin, glucagon Receptor Respose to Receptors on nerve protein chemical stimuli cell membrane Defence protein Structural protein Immunity Support Immunoglobulins Collagen, keratin, elastin

Storage protein Storage of amino Ovalbumin acids

Colloid formation
Globular proteins may be soluble but being macromolecules, they do not dissolve completely in water but form a colloidal solution. Each protein macromolecule is bound by a layer of similar electrical charges which prevent them from settling. Thus, they remain dispersed in water. A layer of water molecules is always found around the protein molecules forming a hydrophilic colloid.

Denaturation of protiens
Denaturation of proteins involves the loss of their specific three-dimensional shape, usually irreversible. Caused by the breakage of the cross linkages when the proteins are exposed to certain extreme conditions but their amino acids sequence remain unchanged. A denatured protein molecule will open up and straighten from the folds to assume a random configuration. Under this condition, it will lose its biological function. Proteins are easily damaged by strong heat with a temperature of greater than 400C.

30

Agents can denature protiens

(a) Heat (b) Strong acids and alkalis / pH (c) Organic solvents and detergents Eg. Benzene & petroleum ether (a) Heavy metals Eg. Mercury and silver ions (b) Radiation, X-ray and radioactive (c) Mechanical force
# A denatured protein can undergo renaturation in favourable condition. The protein will spontaneously refold into its original threedimensional shape.