BIOMOLECULES AND ENZYMES

Detailed explanation-1: -Nonpolar amino acids include alanine (Ala), leucine (Leu), isoleucine (Ile), proline (Pro), tryptophan (Trp), valine (Val), phenylalanine (Phe), and methionine (Met). The side chains of these amino acids are long carbon chains or carbon rings, making them bulky. They are hydrophobic, meaning they repel water.

Detailed explanation-2: -Hydrophobic amino acids have little or no polarity in their side chains. The lack of polarity means they have no way to interact with highly polar water molecules, making them water fearing. There are only five atoms that will appear in your amino acid variable groups: H, C, N, O, and S.

Detailed explanation-3: -Amino acids in each class are in the order of Table 2 : Hydrophobic: A, C, I, L, M, F, W, V. Neutral: G, H, P, S, T, Y. Hydrophilic: R, N, D, Q, E, K.

Detailed explanation-4: -The non-polar amino acids include: alanine, cysteine, glycine, isoleucine, leucine, methionine, phenylalanine, proline, tryptophan, tyrosine and valine. The polar amino acids include: arginine, asparagine, aspartic acid (or aspartate), glutamine, glutamic acid (or glutamate), histidine, lysine, serine, and threonine.

Detailed explanation-5: -Only Ile and Trp are non-polar hydrophobic amino acids present in a pair. For this reason, only these amino acids can participate in hydrophobic interactions with one another.