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Sequence-specific resonance assignment and conformational analysis of subtilin by 2D NMR
W C Chan1, B W Bycroft, M L Leyland
1Department of Pharmaceutical Sciences, University of Nottingham, UK.
FEBS Letters
|March 23, 1992
Abstract:
Subtilin, a 32-amino acid peptide with potent antimicrobial activity, has been isolated from Bacillus subtilis ATCC6633. The chemical structure has been confirmed by the unambiguous sequence-specific assignment of its 1H NMR spectrum. Detailed NMR analysis revealed that subtilin is a rather flexible molecule; the only observed conformational contraints were those imposed by the cyclic structures created by the lanthionine and 3-methyllanthionine residues. These results suggest that in aqueous solution subtilin and the homologous peptide nisin have similar conformations.