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Phosphotyrosine peptide fragmentatio...

Moyer, Susanne Catharine.

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Phosphotyrosine peptide fragmentation by atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Phosphotyrosine peptide fragmentation by atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry./
Author:	Moyer, Susanne Catharine.
Description:	159 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0688.
Contained By:	Dissertation Abstracts International64-02B.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3080729

Phosphotyrosine peptide fragmentation by atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry.
Moyer, Susanne Catharine.

Phosphotyrosine peptide fragmentation by atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry. - 159 p.

Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0688.

Thesis (Ph.D.)--The Johns Hopkins University, 2003.

This work involved the development, fabrication and characterization of an atmospheric pressure matrix-assisted laser desorption/ionization (AP-MALDI) source on an ion trap mass spectrometer. This configuration enables the application-specific selection of external ionization sources: the electrospray/APCI (commercially available) and AP-MALDI (built in-house), which can be readily interchanged within minutes. Experimental evidence suggests that AP-MALDI produces ions with reduced kinetic and internal energies resulting from collisions with ambient gasses. Development of a combination ultraviolet (355 nm) and infrared (2940 nm) AP-MALDI source design allows for MS<super>n</super> analyses of both liquid and solid MALDI samples by ion trap mass spectrometry.Subjects--Topical Terms:

586156
Chemistry, Analytical.

Phosphotyrosine peptide fragmentation by atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry.
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035 $a (UnM)AAI3080729
035 $a AAI3080729
040 $a UnM $c UnM
100 1 $a Moyer, Susanne Catharine. $3 1945908
245 1 0 $a Phosphotyrosine peptide fragmentation by atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry.
300 $a 159 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0688.
500 $a Adviser: Robert J. Cotter.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2003.
520 $a This work involved the development, fabrication and characterization of an atmospheric pressure matrix-assisted laser desorption/ionization (AP-MALDI) source on an ion trap mass spectrometer. This configuration enables the application-specific selection of external ionization sources: the electrospray/APCI (commercially available) and AP-MALDI (built in-house), which can be readily interchanged within minutes. Experimental evidence suggests that AP-MALDI produces ions with reduced kinetic and internal energies resulting from collisions with ambient gasses. Development of a combination ultraviolet (355 nm) and infrared (2940 nm) AP-MALDI source design allows for MS<super>n</super> analyses of both liquid and solid MALDI samples by ion trap mass spectrometry.
520 $a Additionally, an investigation of phosphate loss from phosphopeptide ions was conducted, using both atmospheric pressure matrix-assisted laser desorption/ionization (AP-MALDI) and electrospray ionization (ESI) coupled to an ion trap mass spectrometer (ITMS). These experiments were carried out on a number of phosphorylated peptides in order to investigate gas phase dephosphorylation patterns associated with phosphoserine, phosphothreonine and phosphotyrosine residues. In particular, the fragmentation patterns of phosphotyrosine containing peptides, which experience a loss of 98 Da under CID conditions in the ITMS were explored. This loss of 98 Da is unexpected for phosphotyrosine, given the structure of its side chain. The fragmentation of phosphoserine and phosphothreonine containing peptides was also investigated. While phosphoserine and phosphothreonine residues undergo a loss of 98 Da under CID conditions regardless of peptide amino acid composition, phosphate loss from phosphotyrosine residues seems to be dependent on the presence of arginine or lysine residues in the peptide sequence.
520 $a Additional experiments investigating phosphate loss from sodium-cationized phosphotyrosine containing peptide ions were conducted using liquid infrared (2.94 μm) atmospheric pressure matrix-assisted laser desorption/ionization (AP-MALDI) coupled to an ion trap mass spectrometer (ITMS). In the absence of a basic residue, the protonated phosphotyrosine peptides do not undergo losses of HPO3 (Δ 80 Da) or HPO3 + H2O (Δ 98 Da) in their CID spectra. However, sodium cationized phosphotyrosine containing peptides that do not contain arginine or lysine residues within their sequences do undergo losses of HPO3 (Δ 80 Da) and HPO 3 + H2O (Δ 98 Da) in their CID spectra.
590 $a School code: 0098.
650 4 $a Chemistry, Analytical. $3 586156
650 4 $a Chemistry, Organic. $3 516206
690 $a 0486
690 $a 0490
710 2 0 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 64-02B.
790 1 0 $a Cotter, Robert J., $e advisor
790 $a 0098
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3080729