Phage-Induced Alignment of Membrane Proteins Enables the Measurement and Structural Analysis of Residual Dipolar Couplings with Dipolar Waves and λ-Maps

被引：23

作者：

Park, Sang Ho ^{[1
]}

Son, Woo Sung ^{[1
]}

Mukhopadhyay, Rishi ^{[2
]}

Valafar, Homayoun ^{[2
]}

Opella, Stanley J. ^{[1
]}

机构：

[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

[2] Univ S Carolina, Swearingen Engn Ctr, Columbia, SC 29308 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 40期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

PARAMAGNETIC RELAXATION ENHANCEMENT; NMR STRUCTURE DETERMINATION; POLYACRYLAMIDE-GELS; STRUCTURE REFINEMENT; MICELLES; SPECTROSCOPY; DYNAMICS; HELICES; DNA;

D O I：

10.1021/ja905640d

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

At pH > 6 added filamentous bacteriophage fd is compatible with many of the detergents used to solubilize membrane proteins for solution NMR studies of membrane proteins and, therefore, serves as an alignment media. In combination with strained polyacrylamide get alignment, Dipolar Waves can be used to directly assess the secondary structure and a A-map extracts the order tensors for de novo structure calculation of membrane proteins without distance restraints.

引用

页码：14140 / +

页数：4

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