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Chapter 24: Q23P (page 1283)

After treatment with peroxyformic acid, the peptide hormone vasopressin is partially hydrolyzed. The following fragments are recovered. Propose a structure for vasopressin.

Phe-Gln-Asn Pro-Arg-Gly.NH2 Cys-Tyr-Phe

Asn-Cys-Pro-Arg Tyr-Phe-Gln-Asn

Short Answer

Expert verified

Vasopressin

Step by step solution

01

Step-1. Aligning of fragments of peptide chain:

The structure of vasopressin will be pieced together by at overlaps of the given sequences. For example, Pro-Arg fragment occurs in two sequences, so we align them in such a way that they both overlap with each other. Similarly, for other sequences also.

Alignment of fragments

02

Step-2. Structure of vasopressin:

Structure of vasopressin is obtained by aligning the fragments so that they overlap with each other.

Vasopressin

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Most popular questions from this chapter

Show how you would use bromination followed by amination to synthesize the following amino acids.

  1. Glycine (b) Leucine (c) Glutamic acid

A student took the proton NMR spectrum of phenylalanine in D2Osolution, and had the instrument suppress the DOHsolvent peak. The spectrum is shown below. The integrated relative areas of the peaks are 5:1:1:1.

(a) Draw the structure of phenylalanine as it exists in D2Osolution. (There is a large excess of D2O, and any exchangeable protons in phenylalanine will exchange with the solvent.)

(b) Assign the peaks in the spectrum to the protons in the structure.

(c) Why don’t we see the -NH2or -COOHprotons in the spectrum?

(d) What is the relationship between the two protons that generate nearly mirror-image multiplets at 3.1 and 3.3?

Show where trypsin and chymotrypsin would cleave the following peptide.

Tyr-Ile-Gln-Arg-Leu-Gly-Phe-Lys-Asn-Trp-Phe-Gly-Ala-Lys-Gly-Gln-Gln.NH2

Lipoic acid is often found near the active sites of enzymes, usually bound to the peptide by a long, flexible amide linkage with a lysine residue.

(a) Is lipoic acid a mild oxidizing agent or a mild reducing agent? Draw it in both its oxidized and reduced forms.

(b) Show how lipoic acid might react with two Cys residues to form a disulfide bridge.

(c) Give a balanced equation for the hypothetical oxidation or reduction, as you predicted in part (a), of an aldehyde by lipoic acid.

Histidine is an important catalytic residue found at the active sites of many enzymes. In many cases, histidine appears to remove protons or to transfer protons from one location to another.

(a) Show which nitrogen atom of the histidine heterocycle is basic and which is not.

(b) Use resonance forms to show why the protonated form of histidine is a particularly stable cation.

(c) Show the structure that results when histidine accepts a proton on the basic nitrogen of the heterocycle and then is deprotonated on the other heterocyclic nitrogen. Explain how histidine might function as a pipeline to transfer protons between sites within an enzyme and its substrate.
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