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

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

Full description

Saved in:
Bibliographic Details
Published in:Biophysical journal 2014-08, Vol.107 (4), p.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: Article
Language:English
Subjects:
Escherichia coli
Measles virus - chemistry
Microscopy, Electron, Transmission
Models, Molecular
Nucleocapsid - chemistry
Proteins and Nucleic Acids
Proton Magnetic Resonance Spectroscopy
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:1H-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 1H,15N-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.
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2014.05.048