Conformational Changes in Rhodopsin Probed by Surface Plasmon Resonance Spectroscopy

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

Research output: Contribution to journalArticle

75 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)13706-13711
Number of pages6
JournalBiochemistry
Volume33
Issue number46
DOIs
StatePublished - Nov 1 1994

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Rhodopsin
Surface Plasmon Resonance
Surface plasmon resonance
Spectrum Analysis
Spectroscopy
Proteolipids
Light
Photolysis
Phosphatidylcholines
Silver
GTP-Binding Proteins
Ovum
Irradiation
Technology
Experiments

ASJC Scopus subject areas

  • Biochemistry

Cite this

Conformational Changes in Rhodopsin Probed by Surface Plasmon Resonance Spectroscopy. / Salamon, Z.; Wang, Y.; Brown, Michael F; Macleod, H. A.; Tollin, G.

In: Biochemistry, Vol. 33, No. 46, 01.11.1994, p. 13706-13711.

Research output: Contribution to journalArticle

Salamon, Z. ; Wang, Y. ; Brown, Michael F ; Macleod, H. A. ; Tollin, G. / Conformational Changes in Rhodopsin Probed by Surface Plasmon Resonance Spectroscopy. In: Biochemistry. 1994 ; Vol. 33, No. 46. pp. 13706-13711.
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