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Conformational analysis of bacitracin A, a naturally occurring lariat
Author(s) -
Pons Miquel,
Feliz Miguel,
Molins M. Antònia,
Giralt Ernest
Publication year - 1991
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360310604
Subject(s) - chemistry , bacitracin , moiety , cyclic peptide , molecule , stereochemistry , peptide , crystallography , conformational change , proton nmr , computational chemistry , organic chemistry , biochemistry , antibiotics
The proton nmr spectra of bacitracin A in H 2 O and DMSO‐d 6 have been assigned and the conformational behavior of the peptide in the two solvents has been compared. Although bacitracin A shows a conformational equilibrium between at least two conformations differing in the relative position of the cyclic and linear domains of the molecule, the spectra in water can be interpreted in terms of a preferred conformation in which the linear part is folded over the cyclic moiety and a turn is present around Ile 8 ‐DPhe 9 .