{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["107(4)"],"submitter":["Barbet-Massin E"],"pubmed_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."],"journal":["Biophysical journal"],"pagination":["941-6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4142229"],"repository":["biostudies-literature"],"pubmed_title":["Insights into the structure and dynamics of measles virus nucleocapsids by 1H-detected solid-state NMR."],"pmcid":["PMC4142229"],"pubmed_authors":["Barbet-Massin E","Lesage A","Martinez N","Emsley L","Felletti M","Schneider R","Jensen MR","Ruigrok RW","Communie G","Jehle S","Blackledge M","Pintacuda G"],"additional_accession":[]},"is_claimable":false,"name":"Insights into the structure and dynamics of measles virus nucleocapsids by 1H-detected solid-state NMR.","description":"(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.","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Aug","modification":"2025-04-26T09:08:15.767Z","creation":"2019-03-27T01:34:34Z"},"accession":"S-EPMC4142229","cross_references":{"pubmed":["25140429"],"doi":["10.1016/j.bpj.2014.05.048"]}}