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The conformation of malformin A
Author(s) -
Hall David,
Lyons Paul John,
Pavitt Nicola,
Trezise John A.
Publication year - 1982
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.540030114
Subject(s) - ring (chemistry) , disulfide bond , pentapeptide repeat , chemistry , cystine , molecule , crystallography , nuclear magnetic resonance spectroscopy , stereochemistry , peptide , cysteine , biochemistry , organic chemistry , enzyme
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 SS vibration frequency. The conformation of the backbone, but not that of the disulfide ring, is similar to a model previously proposed.