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 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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Salamon Z,Wang Y,Brown MF,Macleod HA,Tollin Gdoi
10.1021/bi00250a022subject
Has Abstractpub_date
1994-11-22 00:00:00pages
13706-11issue
46eissn
0006-2960issn
1520-4995journal_volume
33pub_type
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