SEQUENCE-SPECIFIC RESONANCE ASSIGNMENT AND CONFORMATIONAL-ANALYSIS OF SUBTILIN BY 2D-NMR

被引：26

作者：

CHAN, WC

BYCROFT, BW

LEYLAND, ML

LIAN, LY

YANG, JC

ROBERTS, GCK

机构：

[1] UNIV NOTTINGHAM,DEPT PHARMACEUT SCI,NOTTINGHAM NG7 2RD,ENGLAND

[2] UNIV LEICESTER,DEPT BIOCHEM,LEICESTER LE1 9HN,ENGLAND

[3] UNIV LEICESTER,CTR BIOL NMR,LEICESTER LE1 9HN,ENGLAND

来源：

FEBS LETTERS | 1992年 / 300卷 / 01期

关键词：

SUBTILIN; LANTIBIOTICS; HPLC; NMR; PEPTIDE CONFORMATION;

D O I：

10.1016/0014-5793(92)80163-B

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：56 / 62

页数：7

共 13 条

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