Magic angle spinning NMR spectroscopy guided atomistic characterization of structure and dynamics in HIV-1 protein assemblies

被引:1
|
作者
Gupta, Rupal [2 ]
Polenova, Tatyana [1 ]
机构
[1] Univ Delaware, Dept Chem & Biochem, Newark, DE 19716 USA
[2] CUNY Coll Staten Isl, Dept Chem, 2800 Victory Blvd, Staten Isl, NY 10304 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
Magic angle spinning; Capsid protein; HIV-1 protein assemblies; SOLID-STATE NMR; NUCLEAR-MAGNETIC-RESONANCE; CHEMICAL-SHIFT ANISOTROPY; CAPSID PROTEIN; TYPE-1; GAG; MAS NMR; MATURATION INHIBITOR; ROTATIONAL RESONANCE; DIMERIZATION DOMAIN; IN-VITRO;
D O I
10.1016/j.cocis.2017.12.005
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Since its discovery, human immunodeficiency virus (HIV) has been an intense subject of research. Several biophysical methodologies have aided towards understanding of the viral lifecycle and infectivity. Magic angle spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy has played a pivotal role in several key findings, providing atomistic details about the viral particles. These contributions have been made owing to tremendous advancements in NMR instrumentation, development of novel experiments and hybrid approaches combining NMR and computational methodologies. In this review, we highlight some advances made towards characterization of structure and dynamics in HIV-1 assemblies by MAS NMR spectroscopy. These findings have established MAS NMR spectroscopy is a promising methodology to investigate large biological assemblies such as viral particles and HIV-1 protein assemblies.
引用
收藏
页码:19 / 34
页数:16
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