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.

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页码：11422 / 11423

页数：2

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