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Models for the structure of outer-membrane proteins of Escherichia coli derived from raman spectroscopy and prediction methods.

Abstract：

:The secondary structure of porin, maltoporin and OmpA protein reconstituted in lipid membranes is determined by Raman spectroscopy. The three proteins have similar structures consisting of 50 to 60% beta-strand, about 20% beta-turn, and less than 15% alpha-helix. Employing a method for structural prediction that accounts for amphipathic beta-strands, folding models are developed for porin and for the segment of OmpA protein incorporated into the membrane. In the model, the OmpA fragment consists of eight amphipathic membrane-spanning beta-strands that form a beta-barrel. Similarly, porin is folded into ten amphipathic membrane-spanning beta-strands that are located at the surface of the trimer towards the lipids and eight predominantly hydrophilic strands in the interior.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Vogel H,Jähnig F

doi

10.1016/0022-2836(86)90292-5

subject

Has Abstract

pub_date

1986-07-20 00:00:00

pages

191-9

issue

2

eissn

0022-2836

issn

1089-8638

pii

0022-2836(86)90292-5

journal_volume

190

pub_type

杂志文章

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