Mixing and Matching Detergents for Membrane Protein NMR Structure Determination

被引：72
|
作者：
Columbus, Linda [1 ,2 ,3 ]
Lipfert, Jan [4 ]
Jambunathan, Kalyani [1 ]
Fox, Daniel A. [1 ]
Sim, Adelene Y. L. [5 ]
Doniach, Sebastian [4 ,5 ,6 ,7 ]
Lesley, Scott A. [2 ,3 ]
机构：
[1] Univ Virginia, Dept Chem, Charlottesville, VA 22904 USA
[2] Scripps Res Inst, Joint Ctr Struct Genom, La Jolla, CA 92037 USA
[3] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA
[4] Stanford Univ, Dept Phys, Stanford, CA 94305 USA
[5] Stanford Univ, Dept Appl Phys, Stanford, CA 94305 USA
[6] Stanford Univ, Biophys Program, Stanford, CA 94305 USA
[7] Stanford Univ, Stanford Synchrotron Radiat Lab, Stanford, CA 94305 USA
来源：
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 21期
基金：
美国国家卫生研究院;
关键词：
NUCLEAR-MAGNETIC-RESONANCE; MOLECULAR-STRUCTURE DETERMINATION; X-RAY-SCATTERING; CRYSTAL-STRUCTURE; XPLOR-NIH; SPIN; SPECTROSCOPY; MICELLES; DIMERIZATION; TRANSPORTER;
D O I：
10.1021/ja808776j
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
One major obstacle to membrane protein structure determination is the selection of a detergent micelle that mimics the native lipid bilayer. Currently, detergents are selected by exhaustive screening because the effects of protein-detergent interactions on protein structure are poorly understood. In this study, the structure and dynamics of an integral membrane protein in different detergents is investigated by nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy and small-angle X-ray scattering (SAXS). The results suggest that matching of the micelle dimensions to the protein's hydrophobic surface avoids exchange processes that reduce the completeness of the NMR observations. Based on these dimensions, several mixed micelles were designed that improved the completeness of NMR observations. These findings provide a basis for the rational design of mixed micelles that may advance membrane protein structure determination by NMR.
引用
收藏
页码：7320 / 7326
页数：7
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