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The conformation of malformin A

✍ Scribed by David Hall; Paul John Lyons; Nicola Pavitt; John A. Trezise

Publisher
John Wiley and Sons
Year
1982
Tongue
English
Weight
496 KB
Volume
3
Category
Article
ISSN
0192-8651

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✦ Synopsis

Abstract

The conformation of the cyclic pentapeptide malformin A has been deduced by systematically generating possible models for the molecule, and minimizing the conformation energy of each. Only one of the low‐energy solutions is fully consistent with the reported CD and NMR spectra, and this is the proposed model. The disulfide ring linking adjacent cystine residues is highly strained, as has been predicted from the Sο£ΏS vibration frequency. The conformation of the backbone, but not that of the disulfide ring, is similar to a model previously proposed.

πŸ“œ SIMILAR VOLUMES

The solution conformation of malformin A
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