Conformational Changes in Rhodopsin Probed by Surface Plasmon Resonance Spectroscopy

Z. Salamon; Y. Wang; M. F. Brown; H. A. Macleod; G. Tollin

doi:10.1021/bi00250a022

Conformational Changes in Rhodopsin Probed by Surface Plasmon Resonance Spectroscopy

Z. Salamon, Y. Wang, M. F. Brown, H. A. Macleod, G. Tollin

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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)
Pages (from-to)	13706-13711
Number of pages	6
Journal	Biochemistry
Volume	33
Issue number	46
DOIs	https://doi.org/10.1021/bi00250a022
State	Published - Nov 1 1994

ASJC Scopus subject areas

Biochemistry

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title = "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 {\AA} 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.",

author = "Z. Salamon and Y. Wang and Brown, {M. F.} and Macleod, {H. A.} and G. Tollin",

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AU - Salamon, Z.

AU - Wang, Y.

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AU - Tollin, G.

PY - 1994/11/1

Y1 - 1994/11/1

N2 - 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.

AB - 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.

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Conformational Changes in Rhodopsin Probed by Surface Plasmon Resonance Spectroscopy

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