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Conformation of malformin A: A proton magnetic resonance and a circular dichroism study

✍ Scribed by Marius Ptak


Publisher
Wiley (John Wiley & Sons)
Year
1973
Tongue
English
Weight
785 KB
Volume
12
Category
Article
ISSN
0006-3525

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✦ Synopsis


Abstract

Malformin A is a cyclic pentapeptide with an intramolecular disulfide bridge. The conformation in solution of this molecule has been studied by NMR and CD. The 270 MHz Proton spectrum in dimethyl sulfoxide is well resolved and the peaks corresponding to the five residues have been assigned.

From the temperature dependence of chemical shifts of the peptide protons and from the exchange rate of these protons, it is concluded that the NH proton of one Cys is shielded from the solvent. This observation and HN~α~CH angles, estimated from the corresponding coupling constants, a proposed conformation of the peptide backbone. From the H~β~C~α~CH coupling constants, a P chirality for the disulfide bridge is proposed. Such a conformation is confirmed by the circular dichroism spectrum which shows a negative band at λ > 250 nm.

It is concluded that the conformation of malformin A is rigid and that the disulfide bridge is exposed to interact with biological receptors.


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