Chapter 29: Q37P (page 1192)
What is the predominant form of each of the following amino acids at pH=11? What is the overall charge on the amino acid? (a)valine; (b)proline; (c)glutamic acid; (d)lysine?
Chapter 29: Q37P (page 1192)
What is the predominant form of each of the following amino acids at pH=11? What is the overall charge on the amino acid? (a)valine; (b)proline; (c)glutamic acid; (d)lysine?
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Get started for freeUse 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.
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.
What amino acid is formed when CH3CONHCH(CO2Et)2is treated with the following series of reagents:
Tryptophan is not classified as a basic amino acid even though it has a heterocycle containing a nitrogen atom. Why is the N atom in the five-membered ring of tryptophan not readily protonated by acid?
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?
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