Chapter 29: 61P (page 1196)
Draw all the steps in the synthesis of each peptide from individual amino acids:
Gly-Ala;
- Ile-Ala-Phe
Short Answer

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Chapter 29: 61P (page 1196)
Draw all the steps in the synthesis of each peptide from individual amino acids:
Gly-Ala;

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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.
Write out a stepwise sequence that shows how a racemic mixture of leucine enantiomers can be resolved into optically active amino acids using .
a. Draw the structure of the tripeptide A-A-A, and label the two ionizable functional groups.
b. What is the predominant form of A-A-A at pH=1?
c. The values for the two ionizable functional groups (3.39 and 8.03) differ considerably from the values of alanine (2.35 and 9.87;see table 29.1). Account for the observed differences.
As shown in Mechanism 29.2, the final steps in the Edman degradation result in rearrangement of a thiazolinone to an N-phenylthiohydantoin. Draw a stepwise mechanism for this acid-catalyzed reaction.

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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