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Chapter 21: Q28P (page 1004)

Which bonds in the backbone of a peptide can rotate freely?

Short Answer

Expert verified

The partial double-bond character prevents free rotation about the peptide bond, so the carbon and nitrogen atoms of the peptide bond and the two atoms to which each is attached are held rigidly in a plane. This regional planarity affects the way a chain of amino acids can fold.

Step by step solution

01

Step-by-step-solutionStep 1: Rotation around peptide bond

The partial double-bond character prevents free rotation about the peptide bond, so the carbon and nitrogen atoms of the peptide bond and the two atoms to which each is attached are held rigidly in a plane. This regional planarity affects the way a chain of amino acids can fold.

02

Backbone of a peptide

The alpha carbon (伪-carbon or C伪) is what connects the amino group to the acid carboxyl group. The bonds on either side of the 伪-carbon in the backbone of a peptide can freely rotate.

Backbone of a peptide

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Most popular questions from this chapter

A mixture of amino acids that do not separate sufficiently when a single technique is used can often be separated by two-dimensional chromatography.In this technique, the mixture of amino acids is applied to a piece of filter paper and separated by chromatographic techniques. The paper is then rotated90掳,and the amino acids are further separated by electrophoresis, producing a type of chromatogram called a fingerprint.Identify the spots in the fingerprint obtainedfrom a mixture of Ser, Glu, Leu, His, Met, and Thr.

Alanine has pKa values of 2.34 and 9.69. Therefore, alanine exists predominately as a zwitterion in an aqueous solution with pH > ____ and pH < ____.

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?

a. Which isomer鈥�(R)-alanine or (S)-alanine鈥攊s d-alanine?

b. Which isomer鈥�(R)-aspartate or (S)-aspartate鈥攊s d-aspartate?

c. Can a general statement be made relating R and S to d and l?

What amino acid is formed using the N-phthalimidomalonic ester synthesis when the following alkyl halides are used in the third step?

(a)

(b)CH3SCH2CH2Br
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