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.
Institute of Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8566, Japan. moto.shibakami@aist.go.jp
Motonari
M
Shibakami
Hisayoshi
H
Tsuihiji
Shin
S
Miyoshi
Makoto
M
Nakamura
Rie
R
Goto
Shigeki
S
Mitaku
Masashi
M
Sonoyama
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