All are involved in stabilizing teiary structure of protein
Teiary structure: The polypeptide chain with secondary structure mentioned above may be fuher folded, super folded twisted about itself forming many sizes. Such a structural conformation is called teiary structure. It is only one such conformation which is biologically active and protein in this conformation is called as the native protein. Thus the teiary structure is constituted by steric relationship between the amino acids located far apa but brought closer by folding. The bonds responsible for interaction between groups of amino acids are as follows: * Hydrophobic interactions: Normally occur between nonpolar side chains of amino acids such as alanine, leucine, methionine, isoleucine, and phenylalanine. They constitute the major stabilizing forces for teiary structure forming a compact three-dimensional structure. * Hydrogen bonds: Normally formed by the polar side chains of the amino acids. * Ionic or electrostatic interactions: These are formed between oppositely charged polar side chains of amino acids, such as basic and acidic amino acids. * Van der Waal Forces: Occur between nonpolar side chains. * Disulfide bonds: These are the SS bonds betweenRef: Textbook of medical biochemistry, MN Chatterji, 8th edition, page no: 91
Hydrogen bond
Hydrophobic interaction
Peptide bond
Van der Waals
Structure and function of protein