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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(a) What is the net charge at neutral pH of a tripeptide containing only alanine? (b) How does the total number of negative and positive charges change following hydrolysis of the tripeptide?
Taurine (2-aminoethanesulfonic acid) is sometimes called an amino acid.
(a) Explain why this designation is not valid. (b) From which of the 20 standard amino acids is taurine derived? Describe the chemical change(s) that occurred.
Identify all the chiral carbons in the amino acids shown in Table 4-1.
Describe how each of the amino acid modifications shown in Fig. 4-14 would affect theof a peptide containing that modified amino acid residue.
What is the approximate net charge of carnosine (a) at pH 3, (b) pH 5,
(c) pH 7, and (d) pH 9?
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