Abstract
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 Å 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 membraneassociated receptors such as rhodopsin.
Original language | English (US) |
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Pages (from-to) | 13706-13711 |
Number of pages | 6 |
Journal | Biochemistry |
Volume | 33 |
Issue number | 46 |
DOIs | |
State | Published - Nov 1 1994 |
ASJC Scopus subject areas
- Biochemistry