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- W2893373722 abstract "The Zika virus (ZIKV) genome encodes a polyprotein that can be post-translationally processed into functional viral proteins. The viral protease is indispensable in the maturation of viral proteins. The Zika protease comprises of two components crucial for catalysis. The N-terminal region of NS3 contains the catalytic triad and approximately 40 amino acids of NS2B are essential for folding and protease activity. NS2B is a membrane protein with transmembrane domains that are critical for the localization of NS3 to the membrane. In this study, we expressed and purified full-length NS2B from ZIKV in E. coli. Purified NS2B was then reconstituted into lyso-myristoyl phosphatidylglycerol (LMPG) micelles. It was found that compared to wild type NS2B, NS2B C11S mutation in LMPG exhibited dispersed cross peaks in the 1H15N-HSQC spectrum, thereby suggesting the feasibility for structural characterization using solution NMR spectroscopy." @default.
- W2893373722 created "2018-10-05" @default.
- W2893373722 creator A5003110246 @default.
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- W2893373722 date "2019-02-01" @default.
- W2893373722 modified "2023-10-18" @default.
- W2893373722 title "Expression, purification of Zika virus membrane protein-NS2B in detergent micelles for NMR studies" @default.
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- W2893373722 doi "https://doi.org/10.1016/j.pep.2018.09.013" @default.
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