Interactions with hydrophobic clusters in the urea-unfolded membrane protein OmPX

被引：20

作者：

Hiller, Sebastian ^{[1
,2
,3
]}

Wider, Gerhard ^{[1
,2
,3
]}

Imbach, Lukas L. ^{[1
,2
,3
]}

Wuethrich, Kurt ^{[1
,2
,3
]}

机构：

[1] ETH, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland

[2] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

[3] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 05期

关键词：

hydrophobic effect; lipids; membrane proteins; NMR spectroscopy; protein folding;

D O I：

10.1002/anie.200703367

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A denatured membrane protein in 8 M urea was characterized. Two hydrophobic clusters, separated by 50 amino acids in the polypeptide chain, are shown to bind independently to detergent micelles (see picture). Long-range interactions between the two clusters are not observed. These observations provide new insights into protein folding mechanisms. (Figure Presented). © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

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收藏

页码：977 / 981

页数：5

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