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: -Disulfide bonds make proteins less susceptible to unfolding; typically, they will link-sheets, -helices, and loops, which means that they primarily maintain tertiary structure, not secondary, which refers to local conformations, and is maintained largely by hydrogen bonds.

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: -Tertiary protein domains are formed by combinations of disulfide bonds, hydrogen bonds, ionic bonds, and non-polar hydrophobic interactions.