Theses and Dissertations at Montana State University (MSU)
Permanent URI for this collectionhttps://scholarworks.montana.edu/handle/1/733
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Item Hydrodynamic analysis of human neutrophil N-formyl chemotactic receptor-G protein interactions : mapping of interfacial domains with receptor-mimetic peptides(Montana State University - Bozeman, College of Letters & Science, 1994) Bommakanti, Rajani KanthItem Structural basis of rhodopsin/G protein coupling : biochemical activity of peptide complexes, photo cross-linking, and mass spectrometric analysis(Montana State University - Bozeman, College of Letters & Science, 2001) Kraft, Paul CamilleItem Structure determination of a retinal rod G protein peptide segment bound to rhodopsin by nuclear magnetic resonance spectroscopy(Montana State University - Bozeman, College of Letters & Science, 1994) Furstenau, Julie EgeItem Antibody imprinting studies of rhodopsin : a model G protein-coupled receptor(Montana State University - Bozeman, College of Letters & Science, 2001) Bailey, Brian WilliamItem Spectrophotometric, mass spectrometeric and structural studies of the prototypical G protein coupled receptor rhodopsin(Montana State University - Bozeman, College of Letters & Science, 2007) Angel, Thomas Emil; Chairperson, Graduate Committee: Algirdas J. JesaitisRhodopsin is the integral membrane protein responsible for black and white vision in low light conditions and is found at high concentration in the mammalian retina. Rhodopsin is a prototypical member of the G protein coupled receptor super family that control much of physiology. Improved understanding of rhodopsin signal transduction and amplification via coupling to the heterotrimeric G protein transducin may reveal conserved activation mechanisms that are relevant to other members of the GPCR super family. Described here are several studies that examine the molecular determinants responsible for heterotrimeric G protein coupling to metarhodopsin II, the active photointermediate of bovine rhodopsin. Employing uv-visible spectroscopy we have investigated the nature of the interaction between the C-terminal tail of transducin and metarhodopsin II. We have provided evidence that suggests the orientation of transducin when it interacts with metarhodopsin II.