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Chapter 21: Q26P (page 1004)

Draw the tetrapeptide Ala-Thr-Asp-Asn and indicate the peptide bonds.

Short Answer

Expert verified

Peptide bonds and disulfide bonds are the only covalent bonds that join amino acids together in a peptide or a protein. A tetrapeptide is a peptide that consists of four amino acids that are joined by peptide bonds.

Step by step solution

01

Step-by-step-solutionStep 1: Tetrapeptide

Peptide bonds and disulfide bonds are the only covalent bonds that join amino acids together in a peptide or a protein. A tetrapeptide is a peptide that consists of four amino acids that are joined by peptide bonds.

02

Formation of given tetrapeptide

The given tetrapeptide is formed by the following amino acid, i.e., Alanine, threonine, aspartic acid, and asparagine. These peptides and proteins are written with the free amino group (of the N-terminal amino acid) on the left and the free carboxyl group (of the C-terminalamino acid) on the right.

The given tetrapeptide is formed as follows:

Formation of tetrapeptide

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Most popular questions from this chapter

A decapeptide undergoes partial hydrolysis to give peptides whose amino acid composition is shown. Reaction of the intact decapeptide with Edman鈥檚 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 product obtained when a lysine side chain in a polypeptide reacts with maleic anhydride.

Explain the order of elution (with a buffer of pH 4) of the following pairs of amino acids through a column packed with Dowex 50 (Figure 21.3):

a. aspartate before serine c. valine before leucine

b. serine before alanine d. tyrosine before phenylalanine

Glutathione is a tripeptide whose function is to destroy harmful oxidizing agents in the body. Oxidizing agents are bought to be responsible for some of the effects of aging and to play a causative role in cancer.

Glutathione removes oxidizing agents by reducing them. In the process, glutathione is oxidized, resulting in the formation of a disulphide bond between two glutathione molecules. An enzyme subsequently reduces the disulphide bond, returning glutathione to its original condition so it can react with another oxidizing agent.

a. What amino acids make up glutathione?

b. What is unusual about glutathione鈥檚 structure?

Reaction of a polypeptide with carboxypeptidase A releases Met. The polypeptide undergoes partial hydrolysis to give the following peptides.

What is the sequence of the polypeptide?

1. Ser, Lys, Trp4. Leu, Glu, Ser 7. Glu, His 10. Glu, His, Val

2. Gly, His, Ala 5. Met, Ala, Gly8. Leu, Lys, Trp11. Trp, Leu, Glu

3. Glu, Val, Ser 6. Ser, Lys, Val 9. Lys, Ser 12. Ala, Met
See all solutions

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