Insights into the Structure and Dynamics of Measles Virus Nucleocapsids by 1H-detected Solid-state NMR

被引：27

作者：

Barbet-Massin, Emeline ^{[1
]}

Felletti, Michele ^{[1
]}

Schneider, Robert ^{[2
]}

Jehle, Stefan ^{[1
]}

Communie, Guillaume ^{[2
,3
]}

Martinez, Nicolas ^{[3
]}

Jensen, Malene Ringkjobing ^{[2
]}

Ruigrok, Rob W. H. ^{[3
]}

Emsley, Lyndon ^{[1
]}

Lesage, Anne ^{[1
]}

Blackledge, Martin ^{[2
]}

Pintacuda, Guido ^{[1
]}

机构：

[1] Univ Lyon, Ctr RMN Tres Hauts Champs, Inst Sci Analyt, UMR CNRS 5280,Ecole Normale Super Lyon,UCBL, F-69100 Villeurbanne, France

[2] UJF, CNRS, CEA, Inst Biol Struct, F-38027 Grenoble, France

[3] UJF, CNRS, EMBL, Unit Virus Host Cell Interact, F-38042 Grenoble, France

来源：

BIOPHYSICAL JOURNAL | 2014年 / 107卷 / 04期

关键词：

ANGLE-SPINNING NMR; CAPSID PROTEIN ASSEMBLIES; C-TERMINAL DOMAIN; MEMBRANE-PROTEINS; AMYLOID FIBRILS; SPECTROSCOPY; RESOLUTION; RNA; BINDING; NUCLEOPROTEIN;

D O I：

10.1016/j.bpj.2014.05.048

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

H-1-detected solid-state nuclear magnetic resonance (NMR) experiments are recorded on both intact and trypsin-cleaved sedimented measles virus (MeV) nucleocapsids under ultra-fast magic-angle spinning. High-resolution H-1,N-15-fingerprints allow probing the degree of molecular order and flexibility of individual capsid proteins, providing an exciting atomic-scale complement to electro microscopy (EM) studies of the same systems.

引用

收藏

页码：941 / 946

页数：6

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