QUESTION 15 The side chain of would become hydrophobic if its amino group is removed. O tyrosine O tryptophane lysine isoleucine O serine
The basic knowledge required to classify an amino acid as a hydrophobhic is it's side chain do not like to reside in an aqueous environment. In a protein hydrophobhic amino acids are likely to be found in the interior (buried form).
The side chain of lysine would become hydrophobic if it's amino group is removed.
EXPLANATION:
A lysine side chain contains four methylene, which may undergo hydrophobhic interactions if the charged - NH3+ group is salt-bridged or hydrogen-bonded.
The side chain does have significant hydrophobhic character. Lysines are often found buried with only the amino group exposed to the solvent.
Hence, removal acid group in lysine would make the side chain hydrophobic because the side chain has 3 methylene groups, so that even terminal amino group will be charged under physiological conditions, the side chain does have significant hydrophobhic character.
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