Premium
Directional Self‐assembly in Archaerhodopsin‐Reconstituted Phospholipid Liposomes
Author(s) -
Jia Wu,
Li Huang,
Jian Liu,
Ming Ming,
QingGuo Li,
JianDong Ding
Publication year - 2005
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200590330
Subject(s) - chemistry , liposome , phospholipid , self assembly , nanotechnology , biophysics , combinatorial chemistry , biochemistry , organic chemistry , membrane , biology , materials science
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom