Chapter 29: 29P (page 1191)
Draw the product formed when the following amino acid is treated with each reagent: (a); (b), pyridine; (c) HCl (1 equiv); (d) NaOH (1 equiv); (e).

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Chapter 29: 29P (page 1191)
Draw the product formed when the following amino acid is treated with each reagent: (a); (b), pyridine; (c) HCl (1 equiv); (d) NaOH (1 equiv); (e).




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Deduce 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
Name each peptide using both the three-letter and one-letter abbreviations of the component amino acids.

a.

b.
Besides asymmetric hydrogenation (Section 29.4), several other methods are now available for the synthesis of optically active amino acids. How might a reaction like the Strecker synthesis be adapted to the preparation of chiral amino acids?
What is the structure of each amino acid at its isoelectric point: (a) alanine (b) methionine; (c)aspartic acid; (d) lysine?
Draw the structure of each peptide. Label the N-terminal and C-terminal amino acids and all amide bonds.
a. Val–Glu
b. Gly–His–Leu
c. M–A–T–T
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