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- W186018049 abstract "The G-protein coupled receptor rhodopsin is a classical example of a seven transmembrane helix receptor; it is photoexcited and transmits this light signal to a G-protein mediated cascade. Many components of this receptor-triggered cascade can be purified in their native forms from natural sources making this system most suitable for biophysical studies. A central aspect of cellular signal transduction routes is to understand protein-protein interactions in a quantitative way. Surface plasmon resonance (SPR) spectroscopy is a biosensor-based technique that allows investigating molecular interactions by determining kinetic parameters. We here show how dark-adapted rhodopsin can be immobilized on the sensor chip surface. A laser device implemented in the SPR system allowed us to trigger light-induced conformational changes in rhodopsin and to monitor light-dependent binding of the photoreceptor cell G-protein transducin to rhodopsin. The sensor chip surface can be regenerated and used for several rounds of interaction analysis. Furthermore, illuminated rhodopsin can be regenerated by applying 9-cis-retinal on the sensor chip surface." @default.
- W186018049 created "2016-06-24" @default.
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- W186018049 date "2010-01-01" @default.
- W186018049 modified "2023-09-27" @default.
- W186018049 title "Application of Surface Plasmon Resonance Spectroscopy to Study G-Protein Coupled Receptor Signalling" @default.
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- W186018049 doi "https://doi.org/10.1007/978-1-60761-670-2_17" @default.
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