LEVEL OF ORGANISATION OF PROTEIN

STRUCTURE

PRIMARY STRUCTURE
The

sequence of amino acids in the polypeptide chains. Refers to the sequence of amino acids in a polypeptide chain which is determined genetically by the code found in the DNA. This sequence of amino acids dictates the biological function of a protein.

Primary structure (sequence of amino acids) of lysozyme which consist of a single polypeptide chain of 129 acid residues. The enzyme causes lysis of the bacterial cell wall.

SECONDARY STRUCTURE
The

local spatial arrangement of the backbone atoms without regard for the side chains. Both the oxygen and the nitrogen atoms of the backbone are electronegative, with partial negative charges. The weakly positive hydrogen atom attached to the nitrogen atom has an affinity for the oxygen atom of a nearby peptide bond. Individually, these hydrogen bonds are weak, but because they are repeated many times over a relatively long region of the polypeptide chain, they can support a particular shape for that part of the protein.

(- HELIX)

- helix, a delicate coil held together by hydrogen bonding between every fourth amino acid. Generally, a protein which is entirely made up of - helix structure is stable and fibrous. Example: Keratin which has a structural role and can be found in nails, hair, and horn.

(- PLEATED SHEET)

This structure is formed when some stretched polypeptide chains are arranged parallel to each other and are held together by hydrogen bond and folded longitudinally. - pleated sheet has a high resistance to stretching. Pleated sheets make up the core of many globular proteins. Example: Fibroin, a protein found in silk is entirely of this form.

TERTIARY STRUCTURE
The

3-dimensional arrangement of the entire polypeptide chain including the side chains. Refers to 3-dimensional, compact and globular shape of a polypeptide. The structure is maintained by the interaction of hydrogen bonds, ionic bonds, disulphide bridges and hydrophobic interaction that are formed between the amino acid residues of the polypeptide chain. Example of protein with tertiary structure are enzymes, hormones, antibodies, plasma protein.

Bonds involved in maintaining the secondary, tertiary and quaternary structure of protein.

QUATERNARY STRUCTURE

The association of 2 or more sub-units in 3-dimensional space. Refers to the precise arrangement of more than one polypeptide chain which are held together by hydrogen bonds, ionic bond and hydrophobic interaction. Example of globular protein with such structure is haemoglobin. It consists of four polypeptide subunits, two of one kind ("a chains") and two of another kind (" chains"). Another example is collagen, which is a fibrous protein that has helical subunits intertwined into a larger triple helix, giving the long fibers great strength. This suits collagen fibers to their function as the girders of connective tissue in skin, bone, tendons, ligaments, and other body parts (collagen accounts for 40% of the protein in a human body).

Beta chain

Alpha chain

Heme

Alpha chain Beta chain Haemoglobin, a globular protein, consist of four polypeptide chains, each joined to an iron-containing molecule, a heme. Collagen, a fibrous protein, is a triple helix consisting of three long polypeptide chains.

Fibrous proteins Long parallel polypeptide chains Polypeptide chain form helical structure on pleated sheets held by hydrogen bonds

Globular proteins Coiled and folded into globular shape Globular structure maintained by hydrogen, ionic, disulphide bonds and hydrophobic interactions

Secondary structure most important in carrying out its function - Stable structure - Insoluble in water

Tertiary structure determines its functions Relatively unstable structure - Usually soluble in water, can form colloidal suspension

Examples are keratin, collagen and fibroin

Examples are haemoglobin, myoglobin, enzymes and antibodies

Comparison of fibrous and globular proteins

PROPERTIES OF PROTEIN

COLLOID FORMATION
Globular protein 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 and thus, they remain dispersed in water. A layer of water molecules is always found around the protein molecules forming a hydrophilic colloid.

DENATURATION OF PROTEINS
Denaturation of proteins involves the loss of their specific 3-dimensional shape and is usually irreversible. This is 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 molecules will open up and straighten from the folds to assume a random configuration. Under this condition, it will lose its biological function.

CAUSES OF DENATURATION OF PROTEINS

High temperature Proteins are easily damaged by strong heat with temperature of greater than 40c. Strong acids and alkalis These chemicals will disrupt the ionic bonds at the amino and carboxyl groups and cause the protein to coagulate. Under prolonged condition, the peptide bonds of the polypeptide chain may be broken. Organic solvents and detergents Hydrophobic interactions and hydrogen bonds may be disrupt. These chemicals themselves may form bonds with the nonpolar groups found in the protein concerned.

Heavy metals Ionic bonds are disrupted when cation of the metal bind with negatively charged carboxyl groups of the protein. This will reduce the polarity and solubility of the protein and cause it to precipitate. Radiation - The kinetic energy of radiation causes the atoms of the protein to vibrate strongly and disrupt ionic and hydrogen bonds. The protein then coagulates. Mechanical force Protein, for example: albumen, when beaten turns white and hardened. This is due to the disruption of some of the bonds found in the protein.

RENATURATION OF PROTEIN
Renaturation is the process of returning a denatured protein structure to its original structure and normal level of biological activity, or simply the remodification or folding of an unfolded polypeptide chain of proteins to its normal three-dimensional structure In fact, a renatured protein is able to carry out its functions better, faster and more efficiently, because it is able to pinpoint the level of biological activity that it was going through prior to the process of denaturation.

Denaturation and renaturation of a protein

High temperatures or various chemical treatments will denature a protein, causing it to lose its shape and hence its ability to function. If the denatured protein remains dissolved, it can often renature when the chemical and physical aspects of its environment are restored to normal.