東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Protein functional explorations usin...

Copeland, Jennifer Cheri.

Linked to FindBook

Google Book

Amazon

博客來

Protein functional explorations using mass spectrometry, nuclear magnetic resonance imaging and bioinformatics tools.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Protein functional explorations using mass spectrometry, nuclear magnetic resonance imaging and bioinformatics tools./
Author:	Copeland, Jennifer Cheri.
Description:	126 p.
Notes:	Source: Dissertation Abstracts International, Volume: 74-08(E), Section: B.
Contained By:	Dissertation Abstracts International74-08B(E).
Subject:	Chemistry, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3558775
ISBN:	9781303033476

Protein functional explorations using mass spectrometry, nuclear magnetic resonance imaging and bioinformatics tools.
Copeland, Jennifer Cheri.

Protein functional explorations using mass spectrometry, nuclear magnetic resonance imaging and bioinformatics tools. - 126 p.

Source: Dissertation Abstracts International, Volume: 74-08(E), Section: B.

Thesis (Ph.D.)--The University of Nebraska - Lincoln, 2013.

Proteins are the workhorses of the cells. The Human Genome Project, completed in 2001, opened the pathway to genomic studies, as the knowledge of so many putative proteins sparked the interest of scientists around the world. Whole and partial genomes are completed continually, and there are nearly 28 million putative proteins predicted from these. A rapid approach for dealing with these involves using bioinformatics with sequence and structural homology, but these only help annotate around 60% of the proteins, leaving a large number of proteins that cannot be approached through computation alone.

ISBN: 9781303033476Subjects--Topical Terms:

1021807
Chemistry, General.

Protein functional explorations using mass spectrometry, nuclear magnetic resonance imaging and bioinformatics tools.
LDR:03192nam a2200337 4500 001 1967601
005 20141124080600.5
008 150210s2013 ||||||||||||||||| ||eng d
020 $a 9781303033476
035 $a (MiAaPQ)AAI3558775
035 $a AAI3558775
040 $a MiAaPQ $c MiAaPQ
100 1 $a Copeland, Jennifer Cheri. $3 2104641
245 1 0 $a Protein functional explorations using mass spectrometry, nuclear magnetic resonance imaging and bioinformatics tools.
300 $a 126 p.
500 $a Source: Dissertation Abstracts International, Volume: 74-08(E), Section: B.
500 $a Adviser: Robert Powers.
502 $a Thesis (Ph.D.)--The University of Nebraska - Lincoln, 2013.
520 $a Proteins are the workhorses of the cells. The Human Genome Project, completed in 2001, opened the pathway to genomic studies, as the knowledge of so many putative proteins sparked the interest of scientists around the world. Whole and partial genomes are completed continually, and there are nearly 28 million putative proteins predicted from these. A rapid approach for dealing with these involves using bioinformatics with sequence and structural homology, but these only help annotate around 60% of the proteins, leaving a large number of proteins that cannot be approached through computation alone.
520 $a Biological assays of all of these proteins are cost- and time-consuming and not feasible with this large (and growing) number. High-throughput screening (HTS) techniques have been developed to approach this through a combinatorial approach. These include using highly sensitive analytical detectors like mass spectroscopy (MS) and nuclear magnetic resonance imaging (NMR). This can cut down on the time of analysis, allowing more proteins to be analyzed. Ligands are placed with the protein and interactions are monitored by the detectors.
520 $a The work in this dissertation attempts to combine the approaches of bioinformatics and analytical chemistry to study protein functional relationships. 1D- 1H NMR spectra are analyzed, and interaction is verified with 2D- 15N HSQC experiments.
520 $a The compound library used for these analyses is based on biologically-relevant compounds that are typically small and water soluble. This is the Functional Annotation Screening Technology by NMR (FAST-NMR) process that has been developed. The nature of the protein-ligand binding is probed with Comparison of Active-Site Structures (CPASS), a program and database that searches and aligns protein active sites. The compound library is also used in MS studies, and their applicability to an LC-MS library is discussed.
520 $a CPASS is further discussed, with improvements in calculation and scope being addressed. The potential to use active-site binding information in protein evolutionary studies is also addressed, in relation to common evolutionary determination by sequence and structure alignment.
590 $a School code: 0138.
650 4 $a Chemistry, General. $3 1021807
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Chemistry, Analytical. $3 586156
690 $a 0485
690 $a 0487
690 $a 0486
710 2 $a The University of Nebraska - Lincoln. $b Chemistry. $3 1030646
773 0 $t Dissertation Abstracts International $g 74-08B(E).
790 $a 0138
791 $a Ph.D.
792 $a 2013
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3558775