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Precise and accurate structural geno...

Shen, Yang.

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Precise and accurate structural genomics protein structure determination using RD and GFT NMR spectroscopy.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Precise and accurate structural genomics protein structure determination using RD and GFT NMR spectroscopy./
Author:	Shen, Yang.
Description:	161 p.
Notes:	Advisers: Jim D. Atwood; Thomas Szyperski.
Contained By:	Dissertation Abstracts International66-12B.
Subject:	Chemistry, Physical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3203956
ISBN:	9780542498466

Precise and accurate structural genomics protein structure determination using RD and GFT NMR spectroscopy.
Shen, Yang.

Precise and accurate structural genomics protein structure determination using RD and GFT NMR spectroscopy. - 161 p.

Advisers: Jim D. Atwood; Thomas Szyperski.

Thesis (Ph.D.)--State University of New York at Buffalo, 2006.

Nuclear magnetic resonance (NMR) has emerged as a powerful tool for determining three-dimensional structures of proteins in solution. The major part of this dissertation describes the efforts to deal with the core steps involved in NMR-base protein structure determination: NMR data collection, NMR data analysis, structure calculation and refinement.

ISBN: 9780542498466Subjects--Topical Terms:

560527
Chemistry, Physical.

Precise and accurate structural genomics protein structure determination using RD and GFT NMR spectroscopy.
LDR:02599nam 2200301 a 45 001 967485
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020 $a 9780542498466
035 $a (UMI)AAI3203956
035 $a AAI3203956
040 $a UMI $c UMI
100 1 $a Shen, Yang. $3 1291358
245 1 0 $a Precise and accurate structural genomics protein structure determination using RD and GFT NMR spectroscopy.
300 $a 161 p.
500 $a Advisers: Jim D. Atwood; Thomas Szyperski.
500 $a Source: Dissertation Abstracts International, Volume: 66-12, Section: B, page: 6650.
502 $a Thesis (Ph.D.)--State University of New York at Buffalo, 2006.
520 $a Nuclear magnetic resonance (NMR) has emerged as a powerful tool for determining three-dimensional structures of proteins in solution. The major part of this dissertation describes the efforts to deal with the core steps involved in NMR-base protein structure determination: NMR data collection, NMR data analysis, structure calculation and refinement.
520 $a NMR data collection has been recognized as one of the major bottlenecks of NMR-base structure determination due to the necessarily long time. Chapter 2 and 3 describe two NMR data collection and analysis protocols for high-quality protein structure determination based on Reduced Dimensionality (RD) and G-matrix Fourier transform (GFT) NMR, respectively. The rapidly collected RD & GFT NMR data enabled high-quality structure determination of four structural genomics target proteins in high-throughput. Chapter 5 introduces the program UBNMR which was developed to facilitate NMR data analysis in general and RD & GFT NMR data pre-processing and data analysis in particular. RD and GFT NMR based protocols, with the aid of UBNMR, are expected to greatly impact on the NMR-based structural biology and structural genomics.
520 $a In addition to rapid NMR data collection and analysis, structure calculation and refinement are also pivotal for obtaining the high-quality protein structures. Chapter 5 describes the analysis of the newly implemented simultaneous GFT NOESY to obtain an accurate and precise initial structural fold. Chapter 6 presents a protein structure refinement strategy using NOE data collected in supercooled water at low temperatures.
590 $a School code: 0656.
650 4 $a Chemistry, Physical. $3 560527
690 $a 0494
710 2 0 $a State University of New York at Buffalo. $3 1017814
773 0 $t Dissertation Abstracts International $g 66-12B.
790 $a 0656
790 1 0 $a Atwood, Jim D., $e advisor
790 1 0 $a Szyperski, Thomas, $e advisor
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3203956