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Spectroscopic and electrochemical st...

Davis, Ryan W.

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Spectroscopic and electrochemical studies of membrane proteins in supported bilayer systems.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Spectroscopic and electrochemical studies of membrane proteins in supported bilayer systems./
作者:	Davis, Ryan W.
面頁冊數:	190 p.
附註:	Adviser: James Brozik.
Contained By:	Dissertation Abstracts International68-01B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3249845

Spectroscopic and electrochemical studies of membrane proteins in supported bilayer systems.
Davis, Ryan W.

Spectroscopic and electrochemical studies of membrane proteins in supported bilayer systems. - 190 p.

Adviser: James Brozik.

Thesis (Ph.D.)--The University of New Mexico, 2006.

Integral membrane proteins represent some of the most elusive and interesting structures in biophysics. Although many membrane proteins serve a structural role, membrane protein receptors provide an integral role for communication between a cell and its external environment, making this protein family the predominant target for pharmaceutical development. However, the requisite presence of a biological membrane in these structures has significantly hindered the mechanistic study of these proteins in comparison to their cytosolic counterparts. Among the most severe difficulties encountered in membrane proteins is their resistance to crystallization, which severely restricts the acquisition of high resolution structural data. Overcoming this limitation necessitates the development of innovative biointerfacial platforms for incorporating membrane protein architectures.Subjects--Topical Terms:

1019105
Biophysics, General.

Spectroscopic and electrochemical studies of membrane proteins in supported bilayer systems.
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035 $a (UMI)AAI3249845
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040 $a UMI $c UMI
100 1 $a Davis, Ryan W. $3 1294878
245 1 0 $a Spectroscopic and electrochemical studies of membrane proteins in supported bilayer systems.
300 $a 190 p.
500 $a Adviser: James Brozik.
500 $a Source: Dissertation Abstracts International, Volume: 68-01, Section: B, page: 0306.
502 $a Thesis (Ph.D.)--The University of New Mexico, 2006.
520 $a Integral membrane proteins represent some of the most elusive and interesting structures in biophysics. Although many membrane proteins serve a structural role, membrane protein receptors provide an integral role for communication between a cell and its external environment, making this protein family the predominant target for pharmaceutical development. However, the requisite presence of a biological membrane in these structures has significantly hindered the mechanistic study of these proteins in comparison to their cytosolic counterparts. Among the most severe difficulties encountered in membrane proteins is their resistance to crystallization, which severely restricts the acquisition of high resolution structural data. Overcoming this limitation necessitates the development of innovative biointerfacial platforms for incorporating membrane protein architectures.
520 $a In order to better interrogate the fundamental structural dynamics of ion channels and membrane bound proteins in general, this work describes recently developed solid - supported lipid bilayer platforms in which membrane bound proteins can be electrochemically and optically interrogated. Using planar and high curvature porous silica membrane supports, several basic studies on symmetric and asymmetric supported lipid bilayers were performed. These studies provide important results in understanding the morphology and stability of different biomimetic membranes under various substrate conditions. Notable observations include a supported bilayer stability gradient resulting from increasing substrate curvature and pore size, suspended fluid bilayers over pores with diameters less than twice the bilayer thickness, and supported bilayer - detergent interactions comparable to solution state bilayers.
520 $a Using novel and established methods of protein incorporation in these bilayers resulted in biophysical studies on several antimicrobial peptides, the light-driven proton pump, bacteriorhodopsin, and the elusive serotonin type 3 ligand - gated ion channel. The silica substrates employed in these studies provided ideal optical properties for a variety of fluorescence experiments, employing fluorescent conjugates of membrane components, proteins, and ligands. In the case of the antimicrobial peptide, gramicidin, single molecule fluorescence imaging was used to identify monomeric and dimeric ion channel states, leading to the elucidation of the standard thermodynamic quantities of this important model system. In the case of the serotonin type 3 receptor (5HT3R), calcium release from a nanoporous microbead supported bilayer was used to demonstrate the function of this complex ligand - gated ion channel in a biomimetic environment. Additional results include an increase in overall right - side - out orientation of bacteriorhopsin and 5HT3R in supported membranes introduced by a novel direct reconstitution method. Complementary computational studies using structures homologous to 5HT3R were employed to gain a better understanding of the spatial organization and energetics of ligand binding as well as a hypothetical intermediate structure in this family of membrane receptors.
520 $a The potential impact of combined optical and electrochemical measurements goes well beyond the study of basic biophysical mechanisms. This strategy can provide significant technological benefit. In biodetection, for example, this scheme offers the specificity of biochemical interactions, the sensitivity of single molecule fluorescence detection, and the amplification afforded by the opening of a membrane channel. In medicinal chemistry, similar strategies provide new ways of testing drug candidates under high - throughput conditions.
590 $a School code: 0142.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Physical. $3 560527
690 $a 0494
690 $a 0786
710 2 0 $a The University of New Mexico. $3 1018024
773 0 $t Dissertation Abstracts International $g 68-01B.
790 $a 0142
790 1 0 $a Brozik, James, $e advisor
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3249845