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Insights into the structure and dynamics of measles virus nucleocapsids by 1H-detected solid-state NMR.

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.

SUBMITTER: Barbet-Massin E

PROVIDER: S-EPMC4142229 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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Insights into the structure and dynamics of measles virus nucleocapsids by 1H-detected solid-state NMR.

Barbet-Massin Emeline E Felletti Michele M Schneider Robert R Jehle Stefan S Communie Guillaume G Martinez Nicolas N Jensen Malene Ringkjøbing MR Ruigrok Rob W H RW Emsley Lyndon L Lesage Anne A Blackledge Martin M Pintacuda Guido G

Biophysical journal 20140801 4

(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. ...[more]

PMID: 25140429

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