Chapter 29: Q53. (page 1194)
Name each peptide using both the three-letter and one-letter abbreviations of the component amino acids.

Short Answer
1.Gly-Asp-Glu and G-D-E.
2.Ala-Gly-Arg and A-G-R.
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Chapter 29: Q53. (page 1194)
Name each peptide using both the three-letter and one-letter abbreviations of the component amino acids.

1.Gly-Asp-Glu and G-D-E.
2.Ala-Gly-Arg and A-G-R.
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Use the given experimental data to deduce the sequence of an octapeptide that contains the following amino acids: Ala, Gly (2 equiv), His (2 equiv), Ile, Leu and Phe. Edman degradation cleaves Gly from the octapeptide, and carboxypeptidase forms Leu and a heptapeptide. Partial hydrolysis forms the following fragments: Ile-His-Leu, Gly, Gly-Ala-Phe-His, and Phe-His-Ile.
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
Histidine is classified as a basic amino acid because one of the N atoms in its five-membered ring is readily protonated by acid. Which N atom in histidine is protonated and why?
(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
Glutathione, a powerful antioxidant that destroys harmful oxidizing agents in cells, is composed of glutamic acid, cysteine, and glycine, and has the following structure:
Glutathione
a. What product is formed when glutathione reacts with an oxidizing agent?
b. What is unusual about the peptide bond between glutamic acid and cysteine?
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