BIOMOLECULES AND ENZYMES

Detailed explanation-1: -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-2: -The tertiary structure of proteins is determined by a variety of chemical interactions. These include hydrophobic interactions, ionic bonding, hydrogen bonding and disulfide linkages. All of these interactions, weak and strong, determine the final three-dimensional shape of the protein.

Detailed explanation-3: -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-4: -In biology, disulfide bridges formed between thiol groups in two cysteine residues are an important component of the secondary and tertiary structure of proteins.

Detailed explanation-5: -Answer and Explanation: The answer is (c) Tertiary and quaternary. Interactions like hydrogen bonding among amino side chains stabilize the tertiary and quaternary structures of proteins.