Sequence‐specific resonance assignment and conformational analysis of subtilin by 2D NMR
- 23 March 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 300 (1), 56-62
- https://doi.org/10.1016/0014-5793(92)80163-b
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 tanthionine and 3-methyllanthionine residues. These results suggest that in aqueous solution subtilin and the homologous peptide nisin have similar conformation.Keywords
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