Virus Structures and Dynamics by Magic-Angle Spinning NMR

被引:13
|
作者
Porat-Dahlerbruch, Gal [1 ]
Goldbourt, Amir [2 ]
Polenova, Tatyana [1 ,3 ]
机构
[1] Univ Delaware, Dept Chem & Biochem, Newark, DC 19716 USA
[2] Tel Aviv Univ, Sch Chem, IL-6997801 Tel Aviv, Israel
[3] Univ Pittsburgh, Sch Med, Pittsburgh Ctr HIV Prot Interact, Pittsburgh, PA 15261 USA
来源
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
MAS NMR; solid-state NMR; virus assemblies; structure; capsids; dynamics; SOLID-STATE NMR; M2 PROTON CHANNEL; MAGNETIC-RESONANCE SPECTRA; CHEMICAL-SHIFT ASSIGNMENT; INFLUENZA-A; TRANSMEMBRANE DOMAIN; COAT PROTEIN; NUCLEAR-POLARIZATION; LIPID-BILAYERS; FUSION PROTEIN;
D O I
10.1146/annurev-virology-011921-064653
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Techniques for atomic-resolution structural biology have evolved during the past several decades. Breakthroughs in instrumentation, sample preparation, and data analysis that occurred in the past decade have enabled characterization of viruses with an unprecedented level of detail. Here we review the recent advances in magic-angle spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy for structural analysis of viruses and viral assemblies. MAS NMR is a powerful method that yields information on 3D structures and dynamics in a broad range of experimental conditions. After a brief introduction, we discuss recent structural and functional studies of several viruses investigated with atomic resolution at various levels of structural organization, from individual domains of a membrane protein reconstituted into lipid bilayers to virus-like particles and intact viruses. We present examples of the unique information revealed by MAS NMR about drug binding, conduction mechanisms, interactions with cellular host factors, and DNA packaging in biologically relevant environments that are inaccessible by other methods.
引用
收藏
页码:219 / 237
页数:19
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