Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/52479
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Type: Journal article
Title: Negative ion fragmentations of deprotonated peptides containing post-translational modifications: diphosphorylated systems containing Ser, Thr and Tyr. A characteristic phosphate/phosphate cyclisation. A joint experimental and theoretical study
Author: Andreazza, H.
Wang, T.
Bilusich, D.
Hoffmann, P.
Bowie, J.
Citation: Rapid Communications in Mass Spectrometry, 2009; 23(12):1825-1833
Publisher: John Wiley & Sons Ltd
Issue Date: 2009
ISSN: 0951-4198
1097-0231
Statement of
Responsibility: 
Hayley J. Andreazza, Tianfang Wang, Daniel Bilusich, Peter Hoffmann and John H. Bowie
Abstract: [M-H](-) anions from small diphosphopeptides (phosphate groups on Ser, Thr or Tyr) show characteristic peaks corresponding to m/z 177 (H(3)P(2)O(7) (-)), 159 (HP(2)O(6) (-)) and sometimes [(M-H)(-)-H(4)P(2)O(7)](-). M/z 177 and m/z 159 are major peaks in the spectra of small peptides with 1,2, 1,3, 1,4, 1,5 and 1,6 diphosphate substitution, which means that the decomposing [M-H](-) anions must have flexible structures in order for the two phosphate groups to interact with each other. Peptides where the two phosphate groups are more than six amino acid residues apart have not been studied. Theoretical calculations indicate that m/z 177 is formed in a strongly exothermic reaction involving facile nucleophilic interaction between the two phosphate groups: m/z 159 is formed by loss of water from energised m/z 177.
Keywords: Ions
Phosphates
Tyrosine
Threonine
Serine
Peptides
Spectrum Analysis
Protein Processing, Post-Translational
Cyclization
Phosphorylation
Tandem Mass Spectrometry
DOI: 10.1002/rcm.4081
Grant ID: ARC
Appears in Collections:Aurora harvest
Chemistry and Physics publications

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