biostudies-literatureUnknown107(4)Barbet-Massin E(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.Biophysical journal941-6https://www.ebi.ac.uk/biostudies/studies/S-EPMC4142229biostudies-literatureInsights into the structure and dynamics of measles virus nucleocapsids by 1H-detected solid-state NMR.PMC4142229Barbet-Massin ELesage AMartinez NEmsley LFelletti MSchneider RJensen MRRuigrok RWCommunie GJehle SBlackledge MPintacuda GfalseInsights into the structure and dynamics of measles virus nucleocapsids by 1H-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 flexibility of individual capsid proteins, providing an exciting atomic-scale complement to electro microscopy (EM) studies of the same systems.2014-01-01T00:00:00Z2014 Aug2025-04-26T09:08:15.767Z2019-03-27T01:34:34ZS-EPMC41422292514042910.1016/j.bpj.2014.05.048