BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The hydrophilic amino acids interact more strongly with water (which is polar) than do the hydrophobic amino acids. The interactions of the amino acids within the aqueous environment result in a specific protein shape.

Detailed explanation-2: -The chemical composition of the side chain determines the characteristics of the amino acid. Amino acids such as valine, methionine, and alanine are nonpolar (hydrophobic), while amino acids such as serine, threonine, and cysteine are polar (hydrophilic).

Detailed explanation-3: -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-4: -Where are the stretches of hydrophobic amino acid residues normally found in a globular protein? Hydrophobic amino acids have a hydrophobic core in which the side chains are buried from water, don’t make hydrogen bonds, and this stabilizes the folded state.