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Spectrophotometric, mass spectromete...

Angel, Thomas Emil.

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Spectrophotometric, mass spectrometeric, and structural studies of the prototypical G protein coupled receptor rhodopsin.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Spectrophotometric, mass spectrometeric, and structural studies of the prototypical G protein coupled receptor rhodopsin./
Author:	Angel, Thomas Emil.
Description:	245 p.
Notes:	Advisers: Algirdas J. Jesaitis; Edward A. Dratz.
Contained By:	Dissertation Abstracts International68-02B.
Subject:	Biology, Bioinformatics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3254737

Spectrophotometric, mass spectrometeric, and structural studies of the prototypical G protein coupled receptor rhodopsin.
Angel, Thomas Emil.

Spectrophotometric, mass spectrometeric, and structural studies of the prototypical G protein coupled receptor rhodopsin. - 245 p.

Advisers: Algirdas J. Jesaitis; Edward A. Dratz.

Thesis (Ph.D.)--Montana State University, 2007.

Rhodopsin 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.Subjects--Topical Terms:

1018415
Biology, Bioinformatics.

Spectrophotometric, mass spectrometeric, and structural studies of the prototypical G protein coupled receptor rhodopsin.
LDR:03008nam 2200313 a 45 001 947533
005 20110524
008 110524s2007 ||||||||||||||||| ||eng d
035 $a (UMI)AAI3254737
035 $a AAI3254737
040 $a UMI $c UMI
100 1 $a Angel, Thomas Emil. $3 1271001
245 1 0 $a Spectrophotometric, mass spectrometeric, and structural studies of the prototypical G protein coupled receptor rhodopsin.
300 $a 245 p.
500 $a Advisers: Algirdas J. Jesaitis; Edward A. Dratz.
500 $a Source: Dissertation Abstracts International, Volume: 68-02, Section: B, page: 0945.
502 $a Thesis (Ph.D.)--Montana State University, 2007.
520 $a Rhodopsin 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.
520 $a 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.
520 $a Mass spectrometry is a powerful technique for characterizing intact and digested proteins. We have optimized mass spectral methods for investigating integral membrane proteins, utilizing rhodopsin as a model system. The mass spectrometric studies provide the foundation for future investigations into agonist and antagonist interactions and the related G protein coupled receptors using molecular crosslinking.
520 $a Development and validation of new tools for generating structural constraints for conformational states of proteins that are not amiable to more traditional structural determination techniques are described. Antibody imprinting studies on rhodopsin were advanced with the work presented here. The x-ray crystal structure of the anti-rhodopsin antibody K42-41L in complex with a synthetic epitope mimetic peptide is described. These studies led to the generation of a model of the third cytoplasmic loop of the photointermediate metarhodopsin I and constraints on the conformational changes in metarhodopsin II.
590 $a School code: 0137.
650 4 $a Biology, Bioinformatics. $3 1018415
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0487
690 $a 0715
710 2 $a Montana State University. $3 1255135
773 0 $t Dissertation Abstracts International $g 68-02B.
790 $a 0137
790 1 0 $a Dratz, Edward A., $e advisor
790 1 0 $a Jesaitis, Algirdas J., $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3254737