Transmembrane Protein Activation Refined by Site-Specific Hydration Dynamics

被引：44
|
作者：
Hussain, Sunyia [1 ,2 ]
Franck, John M. [1 ,2 ]
Han, Songi [1 ,2 ]
机构：
[1] Univ Calif Santa Barbara, Dept Chem Engn, Santa Barbara, CA 93016 USA
[2] Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93016 USA
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2013年 / 52卷 / 07期
关键词：
dynamic nuclear polarization; EPR spectroscopy; hydration dynamics; membrane proteins; proteorhodopsin; E-F LOOP; NUCLEAR-POLARIZATION; MOLECULAR-DYNAMICS; INTERHELICAL LOOP; MEMBRANE-PROTEINS; WATER DYNAMICS; SPIN; BACTERIORHODOPSIN; STATE; PROTEORHODOPSIN;
D O I：
10.1002/anie.201206147
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Proteins on film: The Overhauser dynamic nuclear polarization method resolves hydration dynamics to an unprecedented level of detail for a transmembrane protein surface. The heterogeneous hydration landscape of proteorhodopsin rearranges upon photoactivation (see picture), thus providing an insight into how water contributes to protein function even for biological systems embedded in a hydrophobic membrane. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码：1953 / 1958
页数：6
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