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

来源：

CHINESE JOURNAL OF CHEMISTRY | 2005年 / 23卷 / 03期

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

页码：330 / 333

页数：4

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