| Literature DB >> 25140429 |
Emeline Barbet-Massin1, Michele Felletti1, Robert Schneider2, Stefan Jehle1, Guillaume Communie3, Nicolas Martinez4, Malene Ringkjøbing Jensen2, Rob W H Ruigrok4, Lyndon Emsley1, Anne Lesage1, Martin Blackledge2, Guido Pintacuda5.
Abstract
(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.Entities:
Mesh:
Year: 2014 PMID: 25140429 PMCID: PMC4142229 DOI: 10.1016/j.bpj.2014.05.048
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033