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

(1)H-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 (1)H,(15)N-fingerprints allow probing the degree of molecular order and flexibili...

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Published inBiophysical journal Vol. 107; no. 4; pp. 941 - 946
Main Authors Barbet-Massin, Emeline, Felletti, Michele, Schneider, Robert, Jehle, Stefan, Communie, Guillaume, Martinez, Nicolas, Jensen, Malene Ringkjøbing, Ruigrok, Rob W H, Emsley, Lyndon, Lesage, Anne, Blackledge, Martin, Pintacuda, Guido
Format Journal Article
LanguageEnglish
Published Biophysical Society 19.08.2014
Subjects
Analytical chemistry
Chemical Sciences
ANGLE-SPINNING NMR
AMYLOID FIBRILS
SPECTROSCOPY
RNA
NUCLEOPROTEIN
RESOLUTION
C-TERMINAL DOMAIN
CAPSID PROTEIN ASSEMBLIES
MEMBRANE-PROTEINS
BINDING
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Summary:(1)H-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 (1)H,(15)N-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.
Bibliography:PMCID: PMC4142229
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2014.05.048