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Titolo:
SEQUENCE-SPECIFIC RESONANCE ASSIGNMENT AND CONFORMATIONAL-ANALYSIS OFSUBTILIN BY 2D-NMR
Autore:
CHAN WC; BYCROFT BW; LEYLAND ML; LIAN LY; YANG JC; ROBERTS GCK;
Indirizzi:
UNIV NOTTINGHAM,DEPT PHARMACEUT SCI NOTTINGHAM NG7 2RD ENGLAND UNIV LEICESTER,DEPT BIOCHEM LEICESTER LE1 9HN ENGLAND UNIV LEICESTER,CTR BIOL NMR LEICESTER LE1 9HN ENGLAND
Titolo Testata:
FEBS letters
fascicolo: 1, volume: 300, anno: 1992,
pagine: 56 - 62
SICI:
0014-5793(1992)300:1<56:SRAACO>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
NISIN;
Keywords:
SUBTILIN; LANTIBIOTICS; HPLC; NMR; PEPTIDE CONFORMATION;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
13
Recensione:
Indirizzi per estratti:
Citazione:
W.C. Chan et al., "SEQUENCE-SPECIFIC RESONANCE ASSIGNMENT AND CONFORMATIONAL-ANALYSIS OFSUBTILIN BY 2D-NMR", FEBS letters, 300(1), 1992, pp. 56-62

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 H-1 NMR spectrum. Detailed NMR analysis revealed that subtilin is a rather flexible molecule; the only observed conformational constraints 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 08:21:27