Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy

被引：261

作者：

Andronesi, OC

Becker, S

Seidel, K

Heise, H

Young, HS

Baldus, M

机构：

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

[2] Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2005年 / 127卷 / 37期

关键词：

D O I：

10.1021/ja0530164

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments are combined with novel through-bond correlation schemes that probe mobile protein segments. These NMR schemes are demonstrated on a uniformly [C-13, N-15] variant of the 52-residue polypeptide phospholamban. When reconstituted in lipid bilayers, the NMR data are consistent with an a-helical trans-membrane segment and a cytoplasmic domain that exhibits a high degree of structural disorder.

引用

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页码：12965 / 12974

页数：10

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