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Chapter 21: Q36P (page 1012)

Show the steps in the synthesis of the tetrapeptide in problem 34, using Merrifield’s method.

Short Answer

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The answer is,



Reaction

Step by step solution

01

Tetrapeptide

The peptides are the R-CONH-R’ bond and are formed between the amino acid compounds. The peptide chains containing three peptide bonds are called tetrapeptides. The peptide chains always contain peptide bonds a number less than the number of the amino acids used.

02

Explanation

The reaction for the synthesis of tetrapeptide is as given below.

REACTION

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Most popular questions from this chapter

In what order would histidine, serine, aspartate, and valine be eluted with a buffer of pH 4 from a columncontaining an anion-exchange resin (Dowex 1)?

Treatment of a polypeptide with 2-mercaptoethanol yields two polypeptides with the following primary structures:

Val-Met-Tyr-Ala-Cys-Ser-Phe-Ala-Glu-Ser

Ser-Cys-Phe-Lys-Cys-Trp-Lys-Tyr-Cys-Phe-Arg-Cys-Ser

Treatment of the original intact polypeptide with chymotrypsin yields the following peptides:

1. Ala, Glu, Ser 3. Tyr, Val, Met 5. Ser, Phe, 2 Cys, Lys, Ala, Trp

2. 2 Phe, 2 Cys, Ser 4. Arg, Ser, Cys 6. Tyr, Lys

Determine the positions of the disulfide bridges in the original polypeptide.

A decapeptide undergoes partial hydrolysis to give peptides whose amino acid composition is shown. Reaction of the intact decapeptide with Edman’s reagent releases PTH-Gly. What is the sequence of the decapeptide?

1.Ala, Trp

2. Val,Pro,Asp

3. Pro, Val

4. Ala, Glu

5. Trp, Ala, Arg

6.Arg, Gly

7.Glu, Ala, Leu

8. Met, Pro, Leu, Glu

Draw the form of aspartate that predominates at the following pH values:

a. pH = 1.0 b. pH = 2.6 c. pH = 6.0 d. pH = 11.0

Why are buffer solutions of increasingly higher pH used to elute the column that generates the chromatogram shown in Figure 21.5? (Elutemeans wash out with a solvent.)
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