Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa

被引：83

作者：

Sugawara, E ^{[1
]}

Steiert, M ^{[1
]}

Rouhani, S ^{[1
]}

Nikaido, H ^{[1
]}

机构：

[1] UNIV CALIF BERKELEY,GRP BIOPHYS,BERKELEY,CA 94720

来源：

JOURNAL OF BACTERIOLOGY | 1996年 / 178卷 / 20期

关键词：

D O I：

10.1128/jb.178.20.6067-6069.1996

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

When purified without the use of ionic detergents, both OmpA and OprF proteins contained nearly 20% alpha-helical structures, which disappeared completely upon the addition of sodium dodecyl sulfate. This result suggests that the proteins fold in a similar manner, with an N-terminal, membrane-spanning beta-barrel domain and a C-terminal, globular, periplasmic domain.

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页码：6067 / 6069

页数：3

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