Chapter 29: Q51P (page 1194)
Draw the structure for each peptide:
(a) Phe–Ala;
(b) Gly–Gln;
(c) Lys–Gly;
(d) R-H
Short Answer
a.
b.
C.
d.
Chapter 29: Q51P (page 1194)
Draw the structure for each peptide:
(a) Phe–Ala;
(b) Gly–Gln;
(c) Lys–Gly;
(d) R-H
a.
b.
C.
d.
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Get started for freeDeduce the sequence of a heptapeptide that contains the amino acids Ala, Arg, Glu, Gly, Leu, Phe, and Ser, from the following experimental data. Edman degradation cleaves Leu from the heptapeptide, and carboxypeptidase forms Glu and a hexapeptide. Treatment of the heptapeptide with chymotrypsin forms a hexapeptide and a single amino acid. Treatment of the heptapeptide with trypsin forms a pentapeptide and a dipeptide. Partial hydrolysis forms Glu, Leu, Phe, and the tripeptidesGly–Ala–Ser and Ala–Ser–Arg
Question:With reference to the following peptide:
(a) Identify the N-terminal and C-terminal amino acids.
(b) Name the peptide using one-letter abbreviations.
(c) Label all the amide bonds in the peptide backbone.
Draw the organic products formed in each reaction.
a.
b.
(a) What products are formed when each peptide is treated with trypsin? (b) What products are formed when each peptide is treated with chymotrypsin?
[1] Gly–Ala–Phe–Leu–Lys–Ala
[2] Phe–Tyr–Gly–Cys–Arg–Ser
[3] Thr–Pro–Lys–Glu–His–Gly–Phe–Cys–Trp–Val–Val–Phe
Identify the lettered intermediates in the following reaction scheme. This is an alternative method to synthesize amino acids, based on the Gabriel synthesis of 1° amines (Section 25.7A).
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