title: Plasmon-waveguide resonance (PWR) spectroscopy for directly viewing rates of GPCR/G-protein interactions and quantifying affinities.
abstract: Plasmon-waveguide resonance (PWR) spectroscopy is an optical technique that has been developed in our laboratories and applied to the study of membrane-associated proteins, especially GPCRs. It has high sensitivity and requires no labeling of materials, and it can monitor changes in proteolipid mass density and conformation in real time using plasmon excitation by light polarized both perpendicular and parallel to the resonator surface. Direct measurements will be described of the association of ligands and G-proteins to GPCRs incorporated into a self-assembled lipid bilayer deposited on the silica surface of a PWR resonator. These studies have provided new insights into the functioning of this important class of signaling proteins.
authors.affiliation: Department of Chemistry, University of Arizona, Tucson, AZ 85721, USA. hruby@u.arizona.edu
authors.forename: Victor J
authors.initials: VJ
authors.lastname: Hruby
authors.forename: Gordon
authors.initials: G
authors.lastname: Tollin
mesh_terms: D019204:GTP-Binding Proteins / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D011485:Protein Binding; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism*; D013057:Spectrum Analysis / Q000379:methods*; D020349:Surface Plasmon Resonance
chemical_list: D008024:Ligands; D043562:Receptors, G-Protein-Coupled; D019204:GTP-Binding Proteins