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.
引用
收藏
页码：977 / 981
页数：5
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