BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The bonds that provide stabilisation to the tertiary structure of the protein are disulphide bonds, ionic bonds and hydrophobic bonds and wander Waal’s interactions. Myoglobin is an example of the tertiary structure of the protein.

Detailed explanation-2: -Disulfide bonds function to stabilize the tertiary and/or quaternary structures of proteins and may be intra-protein (i.e., stabilizing the folding of a single polypeptide chain) or inter-protein (i.e., multi-subunit proteins such as antibodies or the A and B chains of insulin).

Detailed explanation-3: -Overall, although the hydrophobic effect is the driving force in helping form the tertiary structure of the protein, other interactions such as van der Waals forces, disulfide bonds, hydrogen bonds and ionic interactions also play a role in stabilizing the tertiary structure.