BIOMOLECULES AND ENZYMES

Detailed explanation-1: -H-bonds, electrostatic forces, disulphide linkages, and Vander Waals forces stabilize this structure. The tertiary structure of proteins represents overall folding of the polypeptide chains, further folding of the secondary structure.

Detailed explanation-2: -A disulfide bond is created by two cysteine residues coming together and creating a sulfur-sulfur linkage. This type of linkage contributes to the tertiary structure of proteins.

Detailed explanation-3: -Finally, there’s one special type of covalent bond that can contribute to tertiary structure: the disulfide bond. Disulfide bonds, covalent linkages between the sulfur-containing side chains of cysteines, are much stronger than the other types of bonds that contribute to tertiary structure.

Detailed explanation-4: -Disulfide bonds are important in stabilizing protein quaternary structures.

Detailed explanation-5: -In addition, disulfide bonds are also found in quaternary structure, just like in tertiary structure. Thus, tertiary and quaternary structure both include disulfide bonds.