Conformational changes in rhodopsin probed by surface plasmon resonance spectroscopy.
Surface plasmon resonance (SPR) spectroscopy has been used to follow incorporation and light-induced conformational changes in bovine rhodopsin reconstituted into an egg phosphatidylcholine bilayer deposited on a thin silver film. The magnitude of the SPR spectral changes caused by light varies with pH in a manner paralleling that in flash photolysis experiments, which monitor formation of metarhodopsin II. Irradiation produces an increase of approximately 4 A in the average thickness of the proteolipid layer, consistent with exposure of recognition sites for the G protein. The results demonstrate that the SPR technology described herein may be used to monitor conformational events in membrane-associated receptors such as rhodopsin.
Salamon
Z
Z
Department of Biochemistry, University of Arizona, Tucson 85721.
Wang
Y
Y
Brown
M F
MF
Macleod
H A
HA
Tollin
G
G
D000818:Animals; D002417:Cattle; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000737:chemistry; D008027:Light; D008051:Lipid Bilayers; D011487:Protein Conformation; D012243:Rhodopsin / Q000737:chemistry* / Q000528:radiation effects; D013057:Spectrum Analysis / Q000379:methods
D006898:Hydroxylamines; D008051:Lipid Bilayers; D019811:Hydroxylamine; D012243:Rhodopsin