Conformational changes in rhodopsin probed by surface plasmon resonance spectroscopy.

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

Biochemistry

journal_title

Biochemistry

authors

Salamon Z,Wang Y,Brown MF,Macleod HA,Tollin G

doi

10.1021/bi00250a022

subject

Has Abstract

pub_date

1994-11-22 00:00:00

pages

13706-11

issue

46

eissn

0006-2960

issn

1520-4995

journal_volume

33

pub_type

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