Directional self-assembly in archaerhodopsin-reconstituted phospholipid liposomes

被引:0
|
作者
Wu, J [1 ]
Huang, L
Liu, J
Ming, M
Li, QG
Ding, JD
机构
[1] Fudan Univ, Dept Macromol Sci, Key Lab Mol Engn Polymers, Shanghai 200433, Peoples R China
[2] Fudan Univ, Sch Life Sci, Dept Physiol & Biophys, Shanghai 200433, Peoples R China
关键词
self-assembly; proteoliposome; archaerhodopsin; bacteriorhodopsin; orientation;
D O I
暂无
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
This paper reports, for the first time, that Archaerhodopsin-4 (AR4) could be reconstituted into phospholipid liposomes by self-assembly. AR4 is a new membrane protein isolated from halobacteria H.sp. xz515 in a salt lake of Tibet, China. This is a bacteriorhodopsin (bR) like protein, function as a light-driven proton pump. Experimental measurements verified that similar to bR, AR not only remains its biological activity in proteoliposome, but also keeps a preferred orientation in self-assembly.
引用
收藏
页码:330 / 333
页数:4
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