LIFE SCIENCE

Detailed explanation-1: -The quaternary structure is also stabilized by the non-covalent interactions and disulfide bonds as in the tertiary structure, where more than one polypeptide is held together to form a single functional unit called multimer.

Detailed explanation-2: -Both structures are held in shape by hydrogen bonds, which form between the carbonyl O of one amino acid and the amino H of another.

Detailed explanation-3: -The quaternary structure of a protein is the association of several protein chains or subunits into a closely packed arrangement. Each of the subunits has its own primary, secondary, and tertiary structure. The subunits are held together by hydrogen bonds and van der Waals forces between nonpolar side chains.

Detailed explanation-4: -The Hydrophobic Effect Is a Principal Force Stabilizing Tertiary and Quaternary Structures. In addition to ionic, hydrogen-bonding, and van der Waals interactions, an important driving force for protein folding is the hydrophobic effect.

Detailed explanation-5: -One type of interaction that plays a major role in the correct folding of a protein is the hydrophobic interaction. As a polypeptide folds into its correct shape, amino acids with nonpolar side chains usually cluster at the core of the protein, staying away from water.