Volk David E, Anderson Kurtis M, Gandham Sai H A, May Fiona J, Li Li, Beasley David W C, Barrett Alan D T, Gorenstein David G
Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX 77555-1157, USA.
Biomol NMR Assign. 2008 Dec;2(2):155-7. doi: 10.1007/s12104-008-9109-5. Epub 2008 Aug 12.
Nearly complete backbone and side chain resonance assignments have been obtained for the third domain, residues M289-K400, of the envelope protein from the sylvatic strain (P72-1244) of the dengue 1 virus, containing mutations N336S and E370K, using double- and triple-resonance spectroscopy.
利用双共振和三共振光谱法,已获得登革热1型病毒森林毒株(P72 - 1244)包膜蛋白第三结构域(残基M289 - K400)几乎完整的主链和侧链共振归属,该毒株含有N336S和E370K突变。