3D protein structures by solid-state NMR spectroscopy:: Ready for high resolution

被引：39

作者：

Bockmann, Anja ^{[1
]}

机构：

[1] Univ Lyon 1, CNRS, UMR 5086, Inst Biol & Chim Prot,IFR BioSci 128, F-69367 Lyon, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 33期

关键词：

fibrils; membrane proteins; NMR spectroscopy; protein structures;

D O I：

10.1002/anie.200801352

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) Protocols for determining high-resolution 3D structures of solid proteins are essential for structural studies of fibrils and membrane proteins. Advances in solid-state NMR spectroscopy have led to a multitude of approaches to access restraints and to calculate structures from highly ambiguous data sets. 3D structures at atomic resolution have been derived for several model proteins, as well as for the C-terminal portion of the Het-s prion protein. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：6110 / 6113

页数：4

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