Chapter 4: 10CP (page 94)
List some covalent modifications of amino acids in proteins.
Short Answer
Some covalent modifications of amino acids in proteins are phosphorylation, acetylation, prenylation, and methylation.
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Chapter 4: 10CP (page 94)
List some covalent modifications of amino acids in proteins.
Some covalent modifications of amino acids in proteins are phosphorylation, acetylation, prenylation, and methylation.
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Draw a Cys–Gly–Asn tripeptide. Identify the peptide bond and the N- and C-termini, and determine the peptide’s net charge at neutral pH.
The protein insulin consists of two polypeptides termed the A and B chains. Insulins from different organisms have been isolated and sequenced. Human and duck insulins have the same amino acid sequence with the exception of six amino acid residues, as shown below. Is the pI of human insulin lower than or higher than that of duck insulin?

A sample of the amino acid tyrosine is barely soluble in water. Would a polypeptide containing only Tyr residues, poly(Tyr), be more or less soluble, assuming the total number of Tyr groups remains constant?
List some functions of amino acid derivatives.
Over time, the glutamine residues of polypeptides are susceptible to deamidation, a reaction in which the amide group is replaced by a carboxylate group. What amino acid is produced when glutamine is deamidated?
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