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