![]() ![]() Thus, these proteins show structure-function relationship. For instance, myoglobin and hemoglobin undergo conformational changes when they bind oxygen, therefore they can transport oxygen to the different tissues and lungs respectively. They undergo conformational changes upon ligand binding. Proteins are not entirely rigid molecules. The secondary structures are further folded leading to the formation of higher order structure namely, tertiary structure which is stabilized mainly by hydrogen-bonding, electrostatic interactions, hydrophobic interactions and van der Waals interactions. A protein can acquire a regular secondary structure for instance α-helix, β-pleated sheet, β-turn, and coils. ![]() The amino acids of a protein have been classified as polar, nonpolar, hydrophilic, hydrophobic, acidic, basic, aliphatic and aromatic. ![]() The sequence of amino acids determines each protein's unique 3-dimensional structure and its specific function such as catalysis of biochemical reactions, mechanical support and immune protection, movement, transport of ligand, transmits nerve impulses, and control growth and differentiation. There are 20 different kinds of amino acids that are linked together by peptide bond to make a protein molecule. Proteins are made up of hundreds or thousands of smaller units known as amino acids. ![]()
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