title: Sequence-specific resonance assignment and conformational analysis of subtilin by 2D NMR.
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.
authors.affiliation: Department of Pharmaceutical Sciences, University of Nottingham, UK.
authors.forename: W C
authors.initials: WC
authors.lastname: Chan
authors.forename: B W
authors.initials: BW
authors.lastname: Bycroft
authors.forename: M L
authors.initials: ML
authors.lastname: Leyland
authors.forename: L Y
authors.initials: LY
authors.lastname: Lian
authors.forename: J C
authors.initials: JC
authors.lastname: Yang
authors.forename: G C
authors.initials: GC
authors.lastname: Roberts
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D001426:Bacterial Proteins; D001430:Bacteriocins; D002851:Chromatography, High Pressure Liquid; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010455:Peptides; D010456:Peptides, Cyclic / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation; D012996:Solutions; D013329:Structure-Activity Relationship
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D001430:Bacteriocins; D010455:Peptides; D010456:Peptides, Cyclic; D012996:Solutions; C002836:subtilin