Reconstitution of bacteriorhodopsin into cyclic lipid vesicles.
Bacteriorhodopsin (bR), a membrane protein that can generate a light-driven proton pump, was successfully reconstituted into vesicles composed of an artificial cyclic lipid that mimics archaeal membrane lipids. Unlike reconstituted bR in 1,2-dimyristoyl-sn-glycero-3-phosphocholine vesicles, the net topology and structure of bR molecules in cyclic lipid vesicles are identical to those in the native purple membrane of Halobacterium salinarum.
Shibakami
Motonari
M
Institute of Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8566, Japan. moto.shibakami@aist.go.jp
Tsuihiji
Hisayoshi
H
Miyoshi
Shin
S
Nakamura
Makoto
M
Goto
Rie
R
Mitaku
Shigeki
S
Sonoyama
Masashi
M
D001436:Bacteriorhodopsins / Q000737:chemistry*; D002942:Circular Dichroism; D019617:Halobacterium salinarum / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008055:Lipids / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry*; D013053:Spectrophotometry
D008055:Lipids; D008081:Liposomes; D001436:Bacteriorhodopsins