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The analysis of proteins and peptide...

High, Anthony Andrew.

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The analysis of proteins and peptides by mass spectrometry: From the whole cell proteome to small protein complexes.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	The analysis of proteins and peptides by mass spectrometry: From the whole cell proteome to small protein complexes./
Author:	High, Anthony Andrew.
Description:	128 p.
Notes:	Adviser: Donald F. Hunt.
Contained By:	Dissertation Abstracts International64-01B.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3077313
ISBN:	049397802X

The analysis of proteins and peptides by mass spectrometry: From the whole cell proteome to small protein complexes.
High, Anthony Andrew.

The analysis of proteins and peptides by mass spectrometry: From the whole cell proteome to small protein complexes. - 128 p.

Adviser: Donald F. Hunt.

Thesis (Ph.D.)--University of Virginia, 2003.

Mass spectrometry (MS) is now well established as an extremely powerful analytical tool for protein and peptide analysis, possessing both high-sensitivity and great specificity. It is able to detect signals from as little as 20 attomoles of material. It also possesses the ability to isolate a single species, including post-translational modification on peptides from a background of thousands of co-existing species.

ISBN: 049397802XSubjects--Topical Terms:

586156
Chemistry, Analytical.

The analysis of proteins and peptides by mass spectrometry: From the whole cell proteome to small protein complexes.
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005 20110509
008 110509s2003 eng d
020 $a 049397802X
035 $a (UnM)AAI3077313
035 $a AAI3077313
040 $a UnM $c UnM
100 1 $a High, Anthony Andrew. $3 1258388
245 1 0 $a The analysis of proteins and peptides by mass spectrometry: From the whole cell proteome to small protein complexes.
300 $a 128 p.
500 $a Adviser: Donald F. Hunt.
500 $a Source: Dissertation Abstracts International, Volume: 64-01, Section: B, page: 0177.
502 $a Thesis (Ph.D.)--University of Virginia, 2003.
520 $a Mass spectrometry (MS) is now well established as an extremely powerful analytical tool for protein and peptide analysis, possessing both high-sensitivity and great specificity. It is able to detect signals from as little as 20 attomoles of material. It also possesses the ability to isolate a single species, including post-translational modification on peptides from a background of thousands of co-existing species.
520 $a The techniques of nano-flow RP-HPLC, micro-electrospray quadrupole ion trap mass spectrometry, and Fourier transform ion cyclotron resonance mass spectrometry have been applied to the study of three biological systems. In the first, two-dimensional gel electrophoresis was used to resolve protein spots that mediate estradiol-dependent synaptogenesis in the adult, female rat hippocampus. Understanding what molecules underlie the brain's ability to reconfigure itself will hopefully allow intervention when necessary to reactivate these molecular pathways and reconfigure elements of the central nervous system on demand. Proteolysis in situ with trypsin, followed by mass spectrometry, allowed the identification of both known and novel proteins involved in hippocampal synaptogenesis.
520 $a In the second study, gel electrophoresis was used to resolve proteins co-immunoprecipitating with the FANCA protein from Hela cell extracts. FANCA plays a critical role in the disease Fanconi anemia and is thought to be involved in a novel mechanism for DNA repair. Mass spectrometry allowed the identification of both known and novel molecular partners of FANCA. A novel site of phosphorylation on FANCG, a FANCA binding partner, was identified and its significance verified biochemically.
520 $a In the third study, a methodology is described for identifying proteins from a whole cell proteome involved in the sporulation process of <italic> Bacillus subtilis</italic>. Fourier transform mass spectrometry was used to generate high-resolution mass spectra and a subtractive analysis was performed to identify proteins that characterize stage II spore formation. Understanding how cell differentiation occurs is a necessary step in elucidating how life develops. <italic>Bacillus subtilis</italic> provides a simple model to study cell differentiation.
520 $a In this dissertation, various types of mass spectrometry have been used for subtractive analysis, peptide sequencing, and protein identification in three independent biological systems, demonstrating the importance of mass spectrometry as a tool for discovery.
590 $a School code: 0246.
650 4 $a Chemistry, Analytical. $3 586156
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0486
690 $a 0487
710 2 0 $a University of Virginia. $3 645578
773 0 $t Dissertation Abstracts International $g 64-01B.
790 $a 0246
790 1 0 $a Hunt, Donald F., $e advisor
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3077313