%0 Journal Article
%T NMR Analyses of Fusion Peptide of the Lymantria Dispar Multiple Nucleopolyhedrovirus F Protein<br>杆状病毒蛋白融合肽LdF在溶液中的NMR结构研究
%A XIONG Jing-wen
%A ZENG Dan-yun
%A JIANG Ling
%A LIU Mai-li
%A <br>熊景文
%A 曾丹云
%A 姜凌
%A 刘买利
%J 波谱学杂志
%D 2012
%I 
%X LD130 is the fusion protein of baculoviruse Lymantria dispar multiple nucleopolyhedrovirus (LdMNPV). The N terminal conserved region of subunit F1 in LD130 is the fusion peptide, which actively induces membrane fusion processes. NMR methods were used to identify the solution structure of the fusion peptide under membrane simulated enviornment at low pH. The fusion peptide appeared to be an amphiphilic structure composed of a flexible coil in the N-terminus, and a regular α-helix from L3 to V16. The structure of the LD130 fusion peptide allows us to further investigate the structure-functional relationship of the fusion peptide.
%K NMR
%K structure
%K 2D NMR
%K fusion peptide of baculoviruse<br>核磁共振(NMR)
%K 结构
%K 2D
%K NMR
%K 杆状病毒融合肽
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=6E709DC38FA1D09A4B578DD0906875B5B44D4D294832BB8E&cid=47EA7CFDDEBB28E0&jid=1A3C8C6E452BD1AF5A6B6B99BA3989C9&aid=B39D47F72CB13A76DA021AEB1063F7C2&yid=99E9153A83D4CB11&vid=771469D9D58C34FF&iid=CA4FD0336C81A37A&sid=BFE7933E5EEA150D&eid=5D71B28100102720&journal_id=1000-4556&journal_name=波谱学杂志&referenced_num=0&reference_num=0