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Analysis of three dimensional struct...

Pabuwal, Vagmita.

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Analysis of three dimensional structure of membrane proteins using bioinformatics and computational analysis.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Analysis of three dimensional structure of membrane proteins using bioinformatics and computational analysis./
Author:	Pabuwal, Vagmita.
Description:	103 p.
Notes:	Source: Dissertation Abstracts International, Volume: 71-11, Section: B, page: 6763.
Contained By:	Dissertation Abstracts International71-11B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3430320
ISBN:	9781124296685

Analysis of three dimensional structure of membrane proteins using bioinformatics and computational analysis.
Pabuwal, Vagmita.

Analysis of three dimensional structure of membrane proteins using bioinformatics and computational analysis. - 103 p.

Source: Dissertation Abstracts International, Volume: 71-11, Section: B, page: 6763.

Thesis (Ph.D.)--University of the Sciences in Philadelphia, 2010.

Transmembrane (TM) proteins are estimated to represent &sim;20-30% of the genome and are of great cellular and therapeutical significance. Functioning as receptors, transporters or enzymes, membrane proteins mediate a broad range of fundamental cellular activities. Structure determination of such proteins by experimental methods is very challenging. As a result only a small number of structures are reported. Bioinformatics and computational approaches have proven to be very useful in structure prediction of these proteins. In this thesis we have used these approaches in three different aspects to analyze the 3-dimensional structure of membrane proteins.

ISBN: 9781124296685Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Analysis of three dimensional structure of membrane proteins using bioinformatics and computational analysis.
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020 $a 9781124296685
035 $a (UMI)AAI3430320
035 $a AAI3430320
040 $a UMI $c UMI
100 1 $a Pabuwal, Vagmita. $3 1683938
245 1 0 $a Analysis of three dimensional structure of membrane proteins using bioinformatics and computational analysis.
300 $a 103 p.
500 $a Source: Dissertation Abstracts International, Volume: 71-11, Section: B, page: 6763.
500 $a Adviser: Zhijun Li.
502 $a Thesis (Ph.D.)--University of the Sciences in Philadelphia, 2010.
520 $a Transmembrane (TM) proteins are estimated to represent &sim;20-30% of the genome and are of great cellular and therapeutical significance. Functioning as receptors, transporters or enzymes, membrane proteins mediate a broad range of fundamental cellular activities. Structure determination of such proteins by experimental methods is very challenging. As a result only a small number of structures are reported. Bioinformatics and computational approaches have proven to be very useful in structure prediction of these proteins. In this thesis we have used these approaches in three different aspects to analyze the 3-dimensional structure of membrane proteins.
520 $a For structure prediction of membrane proteins, developing an accurate scoring function for structure discrimination and validation of membrane proteins remains a challenge. Network approaches based on the overall network pattern of residue packing have been proven useful in developing scoring function for soluble protein structure discrimination. This approach has been adopted for membrane proteins. The derived scoring function acts as good indicator of a native fold, and is very effective for discriminating less native membrane protein folds from native ones.
520 $a Elucidating the distinct topology of residue packing in transmembrane proteins is essential for developing high-quality methods for their structure prediction. Along with the network approach, evolutionary conservation of the protein residues and their solvent accessibility was applied on a non-redundant dataset developed for membrane proteins and soluble proteins, in order to understand the packing arrangement of the important residues. Together with the knowledge of a centralized function site for many membrane proteins, a distinct model for membrane proteins was suggested.
520 $a Understanding the structural basis for the ligand-binding selectivity of the seven helical membrane proteins is of significance to their structure prediction. Comparison analysis of proteins' ligand binding sites provides a useful way to study their structure-activity relationships. A pairwise comparison study of the binding sites was done using the seven helical membrane protein structures including the bacteriorhodopsin and the G-protein coupled receptors. This study provided novel insight into the structural basis of ligand-binding selectivity of seven-helical membrane proteins, and is of practical use to the computational modeling of these proteins.
590 $a School code: 1379.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biology, Bioinformatics. $3 1018415
690 $a 0487
690 $a 0715
710 2 $a University of the Sciences in Philadelphia. $3 1017850
773 0 $t Dissertation Abstracts International $g 71-11B.
790 1 0 $a Li, Zhijun, $e advisor
790 $a 1379
791 $a Ph.D.
792 $a 2010
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3430320