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Literature DB >> 10366845

Plasmon resonance spectroscopy: probing molecular interactions within membranes.

Abstract

Surface plasmon resonance (SPR) has become a popular method for investigating biomolecular interactions. A new variant of this technique, coupled plasmon-waveguide resonance (CPWR) spectroscopy, allows the characterization of anisotropic biological membranes. Plasmon resonance can therefore be used to study the molecular events involved in a wide variety of membrane processes, including energy conversion and signal transduction.

Mesh：

Substances：
Rhodopsin

Year: 1999 PMID： 10366845 DOI： 10.1016/s0968-0004(99)01394-8

Source DB: PubMed Journal: Trends Biochem Sci ISSN： 0968-0004 Impact factor: 13.807

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Cited

22 in total

1. Plasmon resonance studies of agonist/antagonist binding to the human delta-opioid receptor: new structural insights into receptor-ligand interactions.

Authors: Z Salamon; S Cowell; E Varga; H I Yamamura; V J Hruby; G Tollin
Journal: Biophys J Date: 2000-11 Impact factor: 4.033

2. Graphical analysis of mass and anisotropy changes observed by plasmon-waveguide resonance spectroscopy can provide useful insights into membrane protein function.

Authors: Zdzislaw Salamon; Gordon Tollin
Journal: Biophys J Date: 2004-04 Impact factor: 4.033

3. Ligand modulation of lateral segregation of a G-protein-coupled receptor into lipid microdomains in sphingomyelin/phosphatidylcholine solid-supported bilayers.

Authors: Isabel D Alves; Zdzislaw Salamon; Victor J Hruby; Gordon Tollin
Journal: Biochemistry Date: 2005-06-28 Impact factor: 3.162

4. Estimation of binding parameters for the protein-protein interaction using a site-directed spin labeling and EPR spectroscopy.

Authors: Marcin Sarewicz; Sebastian Szytuła; Małgorzata Dutka; Artur Osyczka; Wojciech Froncisz
Journal: Eur Biophys J Date: 2007-11-30 Impact factor: 1.733

5. Plasmon waveguide resonance spectroscopic evidence for differential binding of oxidized and reduced Rhodobacter capsulatus cytochrome c2 to the cytochrome bc1 complex mediated by the conformation of the Rieske iron-sulfur protein.

Authors: S Devanathan; Z Salamon; G Tollin; J C Fitch; T E Meyer; E A Berry; M A Cusanovich
Journal: Biochemistry Date: 2007-05-22 Impact factor: 3.162

Review 6. Plasmon-waveguide resonance (PWR) spectroscopy for directly viewing rates of GPCR/G-protein interactions and quantifying affinities.

Authors: Victor J Hruby; Gordon Tollin
Journal: Curr Opin Pharmacol Date: 2007-09-14 Impact factor: 5.547

Plasmon resonance spectroscopy: probing molecular interactions within membranes.

1. Plasmon resonance studies of agonist/antagonist binding to the human delta-opioid receptor: new structural insights into receptor-ligand interactions.

2. Graphical analysis of mass and anisotropy changes observed by plasmon-waveguide resonance spectroscopy can provide useful insights into membrane protein function.

3. Ligand modulation of lateral segregation of a G-protein-coupled receptor into lipid microdomains in sphingomyelin/phosphatidylcholine solid-supported bilayers.

4. Estimation of binding parameters for the protein-protein interaction using a site-directed spin labeling and EPR spectroscopy.

5. Plasmon waveguide resonance spectroscopic evidence for differential binding of oxidized and reduced Rhodobacter capsulatus cytochrome c2 to the cytochrome bc1 complex mediated by the conformation of the Rieske iron-sulfur protein.

Review 6. Plasmon-waveguide resonance (PWR) spectroscopy for directly viewing rates of GPCR/G-protein interactions and quantifying affinities.

7. Curvature forces in membrane lipid-protein interactions.

8. Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes.

9. Unique agonist-bound cannabinoid CB1 receptor conformations indicate agonist specificity in signaling.

Review 10. Retinal dynamics during light activation of rhodopsin revealed by solid-state NMR spectroscopy.