Journal article
Can collision-induced negative-ion fragmentations of [M–H]– anions be used to identify phosphorylation sites in peptides?
Rapid Communications in Mass Spectrometry, Vol.25(23), pp.3537-3548
2011
Abstract
A joint experimental and theoretical investigation of the fragmentation behaviour of energised [M-H]- anions from selected phosphorylated peptides has confirmed some of the most complex rearrangement processes yet to be reported for peptide negative ions. In particular: 1.pSer and pThr (like pTyr) may transfer phosphate groups to C-terminal carboxyl anions and to the carboxyl anion side chains of Asp and Glu, and characteristic nucleophilic/cleavage reactions accompany or follow these rearrangements. 2.pTyr may transfer phosphate to the side chains of Ser and Thr. The reverse reaction, namely transfer of a phosphate group from pSer or pThr to Tyr, is energetically unfavourable in comparison. 3.pSer can transfer phosphate to a non-phosphorylated Ser. The non-rearranged [M-H]- species yields more abundant product anions than its rearranged counterpart. If a peptide containing any or all of Ser, Thr and Tyr is not completely phosphorylated, negative-ion cleavages can determine the number of phosphated residues, and normally the positions of Ser, Thr and Tyr, but not which specific residues are phosphorylated. This is in accord with comments made earlier by Lehmann and coworkers
Details
- Title
- Can collision-induced negative-ion fragmentations of [M–H]– anions be used to identify phosphorylation sites in peptides?
- Authors
- T T Nha Tran (Author) - University of AdelaideTianfang Wang (Author) - University of AdelaideS Hack (Author) - University of AdelaideP Hoffmann (Author) - University of AdelaideJ H Bowie (Author) - University of Adelaide
- Publication details
- Rapid Communications in Mass Spectrometry, Vol.25(23), pp.3537-3548
- Publisher
- John Wiley & Sons Ltd.
- Date published
- 2011
- DOI
- 10.1002/rcm.5261
- 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
- 99450215602621
- Output Type
- Journal article
Metrics
2 File views/ downloads
392 Record Views
InCites Highlights
These are selected metrics from InCites Benchmarking & Analytics tool, related to this output
- Web Of Science research areas
- Biochemical Research Methods
- Chemistry, Analytical
- Spectroscopy
UN Sustainable Development Goals (SDGs)
This output has contributed to the advancement of the following goals:
Source: InCites