Question

Tyrosine and tryptophan are less hydrophobic than phenylalanine because ________. Tyrosine and tryptophan are less hydrophobic than phenylalanine because ________. Phenylalanine has an indole group Phenylalanine is a phenol Tyrosine and tryptophan have smaller R groups Phenylalanine has no polar group in the side chain

Answer 1

Tyrosine and tryptophan are less hydrophobic than phenylalanine because they have polar groups in their side chains, making them more hydrophilic.

Step-by-step explanation:

Tyrosine and tryptophan are less hydrophobic than phenylalanine because tyrosine and tryptophan have polar groups in their side chains, which increases their affinity for water compared to phenylalanine.

Phenylalanine is nonpolar and has no polar group in the side chain, making it more hydrophobic. Tyrosine contains a phenol group in its R group, introducing a polar hydroxyl (-OH) functionality. Tryptophan has an indole group which contains a nitrogen atom, contributing to its relative polarity compared to phenylalanine's purely hydrocarbon side chain. These polar groups make tyrosine and tryptophan more hydrophilic (water-attracting) and thus less hydrophobic than phenylalanine.

Answer 2

Answer: Phenylalanine has no polar group in the side chain

Step-by-step explanation:

Unlike phenylanine with a nonpolar methyl benzyl group in its side chain, tryptothan and tyrosine on the other hand possesses a polar indole ring and hydroxyl group in their side chain respectively, which helps them form hydrogen bonds with water molecules.

Thus, both are less hydrophobic (water-hating) than phenylanine.