BIOMOLECULES AND ENZYMES

Detailed explanation-1: -Also important to tertiary structure are hydrophobic interactions, in which amino acids with nonpolar, hydrophobic R groups cluster together on the inside of the protein, leaving hydrophilic amino acids on the outside to interact with surrounding water molecules.

Detailed explanation-2: -The R-groups of hydrophilic amino acids contain electronegative atoms like O and N. Some amino acids are non-polar (hydrophobic) because their side chains are made up mostly of hydrocarbon chains.

Detailed explanation-3: -On folding, hydrophobic amino acids get buried inside the protein such that they are shielded from the water; this hydrophobic effect makes a protein fold stable.

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.