BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The tertiary structure of a protein refers to the overall three-dimensional arrangement of its polypeptide chain in space. It is generally stabilized by outside polar hydrophilic hydrogen and ionic bond interactions, and internal hydrophobic interactions between nonpolar amino acid side chains (Fig.

Detailed explanation-2: -Image of a hypothetical polypeptide chain, depicting different types of side chain interactions that can contribute to tertiary structure. These include hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridge formation.

Detailed explanation-3: -Four interactions stabilize the tertiary structure of a protein: (a) ionic bonding, (b) hydrogen bonding, (c) disulfide linkages, and (d) dispersion forces. When a protein contains more than one polypeptide chain, each chain is called a subunit.

Detailed explanation-4: -Furthermore, hydrogen bonds and ionic interactions between the polar, charged amino acids contribute to the tertiary structure.

Detailed explanation-5: -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.