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Chapter 29: 19P (page 1170)

Draw the structure of the N-phenylthiohydantoin formed by initial Edman degradation of each peptide: (a) Ala-Gly-Phe-Phe; (b) Val-Ile-Tyr.

Short Answer

Expert verified

Edman degradation is a technique to cleave amino acids from the N-terminal of the peptide chain, and the process continues until the whole sequence is known.

There are two products formed by Edman degradation, one is N-phenylthiohydantoin, and the other is a new peptide chain with one less amino acid.

Step by step solution

01

Edman Degradation

Edman degradation is a technique to cleave amino acids from the N-terminal of the peptide chain, and the process continues until the whole sequence is known.

There are two products formed by Edman degradation, one is N-phenylthiohydantoin, and the other is a new peptide chain with one less amino acid.

02

Structure of the N-phenylthiohydantoin formed by initial Edman degradation of Ala-Gly-Phe-Phe.

a.The initial Edman degradation of Ala-Gly-Phe-Phe is done by cleaving amino acid from N-terminal.

03

Structure of the N-phenylthiohydantoin formed by initial Edman degradation of Val-Ile-Tyr.

b. The initial Edman degradation of Val-Ile-Tyr is done by removing N-terminal amino acid from the peptide chain.

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Most popular questions from this chapter

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.

Give the amino acid sequence of each peptide using the fragments obtained by partial hydrolysis of the peptide with acid.

  1. A tetrapeptide that contains Ala, Gly, His, and Tyr, which is hydrolyzed to the dipeptides His-Tyr, Gly-Ala, and Ala-His.
  2. A pentapeptide that contains Glu, Gly, His, Lys, and Phe, which is hydrolyzed to His-Gly-Glu, Gly-Glu-Phe, and Lys-His.

Draw the structure of each peptide. Label the N-terminal and C-terminal amino acids and all amide bonds.

a. Val鈥揋lu

b. Gly鈥揌is鈥揕eu

c. M鈥揂鈥揟鈥揟

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?

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鈥揂la鈥揝er and Ala鈥揝er鈥揂rg
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