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

H J Andreazza; Tianfang Wang; D Bilusich; P Hoffmann; J H Bowie

doi:10.1002/rcm.4081

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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

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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

H J Andreazza, Tianfang Wang, D Bilusich, P Hoffmann and J H Bowie

Rapid Communications in Mass Spectrometry, Vol.23(12), pp.1825-1833

2009

DOI: https://doi.org/10.1002/rcm.4081

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Abstract

[M-H]- anions from small diphosphopeptides (phosphate groups on Ser, Thr or Tyr) show characteristic peaks corresponding to m/z 177 (H3P2O), 159 (HP2O) and sometimes [(M-H)--H4P2O7]-. 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.

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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
Authors: H J Andreazza (Author) - University of Adelaide
Tianfang Wang (Author) - University of Adelaide
D Bilusich (Author) - University of Adelaide
P Hoffmann (Author) - University of Adelaide
J H Bowie (Author) - University of Adelaide
Publication details: Rapid Communications in Mass Spectrometry, Vol.23(12), pp.1825-1833
Publisher: John Wiley & Sons Ltd.
Date published: 2009
DOI: 10.1002/rcm.4081
ISSN: 0951-4198
Organisation Unit: School of Science and Engineering - Legacy; University of the Sunshine Coast, Queensland; School of Science, Technology and Engineering; Centre for Bioinnovation
Language: English
Record Identifier: 99450230602621
Output Type: Journal article

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