Which amino acid is more soluble in water? Explain why! a. Val b. Tyr c. Ala d.
ID: 96364 • Letter: W
Question
Which amino acid is more soluble in water? Explain why! a. Val b. Tyr c. Ala d. Leu e. Phe Mark each statement below TRUE or FALSE and explain your choice. Credit given only if your reasoning is correct. a) Secondary structures are primarily stabilized by ionic interactions b) Regions of a protein that lack a regular secondary structure are considered denatured c) A single protein can have multiple alpha -helices d) Bends and loops are not important in forming secondary structure A protein is mutated and converts one Asp rightarrow Ala. What effects might this mutation have on the protein structure? Your answer should also explain the impact on each level of protein structure.Explanation / Answer
10) The correct answer is option (b).
The number of alkyl groups present in an amino acid influences their polarity. The more alkyl groups present, the more non-polar the amino acid will be.
Valine, alanine, leucine, and phenylalanine are hydrophobic amino acids whereas tyrosine is a hydrophilic amino acid and is significantly more soluble in water than its precursor, phenylalanine because the hydrogen bonding between the hydroxyl group makes it thermodynamically more stable.
Hydrophobic amino acids are less soluble in water.
11)
a) Secondary structures are primarily stabilized by ionic interactions. False
Secondary structures describe the folding of the polypeptide backbone in a regular coiled pattern and include alpha-helix and beta-sheets which are stabilized by intrachain and interchain hydrogen bonding between N-H and C=O groups.
b) Regions of a protein that lacks a regular secondary structure are considered denatured. True
A denatured protein lacks both tertiary and secondary structure. Denaturation disrupts the hydrogen bonding of alpha-helix and beta sheets which ultimately lead to the distortion of its tertiary structure.
c) A single protein can have multiple alpha-helices. True
A single protein may have multiple alpha-helices as a part of a single polypeptide chain, connected to each other by loops. For example, Interleukin-2 and human Growth Hormone contains four alpha-helices.
d) Bends and loops are not important in forming secondary structure. False
Bends are loops are responsible for linking the regular secondary structure elements i.e alpha-helices and beta-sheets. In the conformational class of proteins, the absence of bends and loops indicates an absence of regular secondary structure. Therefore, they are important.
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