Sequence-specific resonance assignment and conformational analysis of subtilin by 2D NMR

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...

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Veröffentlicht in:	FEBS letters 1992-03, Vol.300 (1), p.56-62
Hauptverfasser:	Chan, Weng C., Bycroft, Barrie W., Leyland, Mark L., Lian, Lu-Yun, Yang, J.C., Roberts, Gordon C.K.
Format:	Artikel
Sprache:	eng
Schlagworte:	2D NMR Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - isolation & purification Anti-Bacterial Agents - metabolism Bacillus subtilis Bacterial Proteins Bacteriocins Biological and medical sciences Chromatography, High Pressure Liquid conformation FAB-MS fast atom bombardment mass spectroscopy Fundamental and applied biological sciences. Psychology HOHAHA homonuclear Hartmann—Hahn HPLC Lantibiotics Magnetic Resonance Spectroscopy Molecular Sequence Data Molecular Structure N.M.R NMR NOESY nuclear Overhauser enhancement spectroscopy Peptide conformation Peptides Peptides, Cyclic - chemistry Peptides, Cyclic - isolation & purification Peptides, Cyclic - metabolism Protein Conformation Proteins reverse-phase high-pressure liquid chromatography RP-HPLC Solutions Structure-Activity Relationship Subtilin two-dimensional nuclear magnetic resonance
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