Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy

被引：72
|
作者：
Giraud, N
Böckmann, A
Lesage, A
Penin, F
Blackledge, M
Emsley, L [1 ]
机构：
[1] Ecole Normale Super Lyon, Chim Lab, CNRS, UMR 5182,ENS,Lab Rech Conventionne,CEA 23V, F-69364 Lyon, France
[2] UCB, Inst Biol & Chim Prot, UMR 5086, CNRS,IFR, F-69367 Lyon, France
[3] UJF, CEA, CNRS, Inst Biol Struct Jean Pierre Ebel, F-38027 Grenoble, France
来源：
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 37期
关键词：
D O I：
10.1021/ja046578g
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a qualitative description of the site-specific internal mobility of the protein present in the solid state. Copyright © 2003 American Chemical Society.
引用
收藏
页码：11422 / 11423
页数：2
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