Structural Rearrangements of Membrane Proteins Probed by Water-Edited Solid-State NMR Spectroscopy

被引：88

作者：

Ader, Christian ^{[1
]}

Schneider, Robert ^{[2
]}

Seidel, Karsten ^{[2
]}

Etzkorn, Manuel ^{[2
]}

Becker, Stefan ^{[2
]}

Baldus, Marc ^{[1
]}

机构：

[1] Univ Utrecht, Bijvoet Ctr Biomol Res, NL-3584 CH Utrecht, Netherlands

[2] Max Planck Inst Biophys Chem, Dept NMR Based Struct Biol, D-37077 Gottingen, Germany

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 01期

关键词：

SPIN-DIFFUSION; K+ CHANNEL; POTASSIUM CHANNEL; CONFORMATIONAL-CHANGES; MOLECULAR-DYNAMICS; KCSA CHANNEL; TOPOLOGY; RELAXATION; RESOLUTION; COMPLEX;

D O I：

10.1021/ja806306e

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We show that water-edited solid-state NMR spectroscopy allows for probing. global protein conformation and residue-specific solvent accessibility in a lipid bilayer environment. The transfer dynamics can be well described by a general time constant, irrespective of protein topology and lipid environment. This approach was used to follow structural changes in response to protein function in the chimeric potassium channel KcsA-Kv1.3. Data obtained as a function of pH link earlier biochemical data to changes in protein structure in a functional bilayer setting.

引用

页码：170 / 176

页数：7

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