東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Facilitation of protein three-dimens...

Pantazatos, Dennis Peter.

FindBook

Google Book

Amazon

博客來

Facilitation of protein three-dimensional structure determination using enhanced peptide amide deuterium exchange mass spectrometry (DXMS).

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Facilitation of protein three-dimensional structure determination using enhanced peptide amide deuterium exchange mass spectrometry (DXMS)./
作者:	Pantazatos, Dennis Peter.
面頁冊數:	269 p.
附註:	Source: Dissertation Abstracts International, Volume: 67-01, Section: B, page: 0252.
Contained By:	Dissertation Abstracts International67-01B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3205364
ISBN:	9780542510922

Facilitation of protein three-dimensional structure determination using enhanced peptide amide deuterium exchange mass spectrometry (DXMS).
Pantazatos, Dennis Peter.

Facilitation of protein three-dimensional structure determination using enhanced peptide amide deuterium exchange mass spectrometry (DXMS). - 269 p.

Source: Dissertation Abstracts International, Volume: 67-01, Section: B, page: 0252.

Thesis (Ph.D.)--University of California, San Diego, 2006.

Three dimensional structure determination and analysis of proteins is necessary for the understanding of how proteins participate in human disease, and are critical for the effective design of therapeutics for clinically important targets. Current efforts for determining protein structures are centered on novel high-throughput (HT) approaches. These include high throughput (HT) crystallization efforts and global structure prediction efforts monitored through the Critical Assessment of Structure Prediction (CASP) experiments where progress has been incremental at best. Protein structure analysis of conformational changes and protein-proteins interactions can be monitored by biophysical methods which include fluorescence spectroscopy, differential scanning calorimetry, circular dichroism and ultra centrifugation. These methods provide adequate low resolution information on global changes in secondary and tertiary structure but are limited in providing detailed information on protein structure, protein conformational changes and protein-protein interactions. Therefore, there is a great need for improvements in the speed and ease of determining and analyzing protein structures and protein dynamics. Hydrogen/Deuterium (H/D) exchange rates are highly dependent on protein structure and amide hydrogen solvent accessibility. Exchange rates can report structure stability at the individual amino acid scale and provide important information on the secondary and tertiary structure.

ISBN: 9780542510922Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Facilitation of protein three-dimensional structure determination using enhanced peptide amide deuterium exchange mass spectrometry (DXMS).
LDR:03761nmm 2200301 4500 001 1827557
005 20070104081203.5
008 130610s2006 eng d
020 $a 9780542510922
035 $a (UnM)AAI3205364
035 $a AAI3205364
040 $a UnM $c UnM
100 1 $a Pantazatos, Dennis Peter. $3 1916483
245 1 0 $a Facilitation of protein three-dimensional structure determination using enhanced peptide amide deuterium exchange mass spectrometry (DXMS).
300 $a 269 p.
500 $a Source: Dissertation Abstracts International, Volume: 67-01, Section: B, page: 0252.
500 $a Adviser: Virgil L. Woods, Jr.
502 $a Thesis (Ph.D.)--University of California, San Diego, 2006.
520 $a Three dimensional structure determination and analysis of proteins is necessary for the understanding of how proteins participate in human disease, and are critical for the effective design of therapeutics for clinically important targets. Current efforts for determining protein structures are centered on novel high-throughput (HT) approaches. These include high throughput (HT) crystallization efforts and global structure prediction efforts monitored through the Critical Assessment of Structure Prediction (CASP) experiments where progress has been incremental at best. Protein structure analysis of conformational changes and protein-proteins interactions can be monitored by biophysical methods which include fluorescence spectroscopy, differential scanning calorimetry, circular dichroism and ultra centrifugation. These methods provide adequate low resolution information on global changes in secondary and tertiary structure but are limited in providing detailed information on protein structure, protein conformational changes and protein-protein interactions. Therefore, there is a great need for improvements in the speed and ease of determining and analyzing protein structures and protein dynamics. Hydrogen/Deuterium (H/D) exchange rates are highly dependent on protein structure and amide hydrogen solvent accessibility. Exchange rates can report structure stability at the individual amino acid scale and provide important information on the secondary and tertiary structure.
520 $a The dissertation is arranged as follows: (1) Chapter 1 is an introduction to Hydrogen/Deuterium exchange mass spectrometry and also reports my studies on the thrombin-Lepirudin complex. (2) Chapter 2 is in preparation for submission and reports the application of DXMS for characterizing the molecular dynamics of spectrin. It also presents the development and validation studies for a computational method for generating amide exchange rate maps from DXMS data, a critical component of the structure determination method described in Chapters six and seven. (3) Chapter 3 reports the application of DXMS for structural analysis of drug-protein interactions. (4) Chapter 4 reports methods for using DXMS to improve the crystallizability of protein constructs for 3D structure determination by x ray crystallography. (5) Chapter 5 reports the detailed 3-D structures of the first two proteins that were successfully studied with the DXMS- guided construct design method. (6) Chapter 6 outlines the development of a hybrid computational-experimental method for high-throughput protein 3-D structure determination: DXMS-Rosetta-COREX engine. (7) Chapter 7 summarizes my conclusions from the foregoing studies and outlines future directions of these studies.
590 $a School code: 0033.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
650 4 $a Biology, General. $3 1018625
690 $a 0487
690 $a 0786
690 $a 0306
710 2 0 $a University of California, San Diego. $3 1018093
773 0 $t Dissertation Abstracts International $g 67-01B.
790 1 0 $a Woods, Virgil L., Jr., $e advisor
790 $a 0033
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3205364