Barbet-Massin Emeline, Felletti Michele, Schneider Robert, Jehle Stefan, Communie Guillaume, Martinez Nicolas, Jensen Malene Ringkjøbing, Ruigrok Rob W H, Emsley Lyndon, Lesage Anne, Blackledge Martin, Pintacuda Guido
Centre de RMN à Très Hauts Champs, Institut des Sciences Analytiques, UMR 5280 CNRS/Ecole Normale Supérieure de Lyon/UCBL, University of Lyon, 69100 Villeurbanne, France.
Institut de Biologie Structurale, CEA, CNRS, UJF, 38027 Grenoble, France.
Biophys J. 2014 Aug 19;107(4):941-6. doi: 10.1016/j.bpj.2014.05.048.
(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.
(1)氢检测固态核磁共振(NMR)实验是在超快速魔角旋转条件下,对完整的和经胰蛋白酶切割的沉降麻疹病毒(MeV)核衣壳进行记录的。高分辨率的氢-氮指纹图谱能够探测单个衣壳蛋白的分子有序度和灵活性,为同一系统的电子显微镜(EM)研究提供了令人兴奋的原子尺度补充。