ArticleJournal of the American Society for Mass Spectrometry2008
The effect of phosphorylation on the electron capture dissociation of peptide ions.
Article in Journal of the American Society for Mass Spectrometry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Characterization of Phosphorylated Peptides by Electron-Activated and Ultraviolet Dissociation Mass Spectrometry: A Comparative Study with Collision-Induced Dissociation.Journal of the American Society for Mass Spectrometry · 2024Article
- Multimodal Tandem Mass Spectrometry Techniques for the Analysis of Phosphopeptides.Journal of the American Society for Mass Spectrometry · 2022Article
- Structural Analysis of 14-3-3-ζ-Derived Phosphopeptides Using Electron Capture Dissociation Mass Spectrometry, Traveling Wave Ion Mobility Spectrometry, and Molecular Modeling.The journal of physical chemistry. B · 2020Article
- Phosphopeptide Fragmentation and Site Localization by Mass Spectrometry: An Update.Analytical chemistry · 2019Review
- Electron transfer dissociation mass spectrometry of acidic phosphorylated peptides cationized with trivalent praseodymium.Journal of mass spectrometry : JMS · 2018Article
- Replacing HChemical science · 2018Article
- The Impact of Phosphorylation on Electron Capture Dissociation of Proteins: A Top-Down Perspective.Journal of the American Society for Mass Spectrometry · 2017Article
- Effects of acidic peptide size and sequence on trivalent praseodymium adduction and electron transfer dissociation mass spectrometry.Journal of mass spectrometry : JMS · 2017Article
- Characterisation of phosphorylated nucleotides by collisional and electron-based tandem mass spectrometry.Rapid communications in mass spectrometry : RCM · 2016Article
- Electron Capture Dissociation of Sodium-Adducted Peptides on a Modified Quadrupole/Time-of-Flight Mass Spectrometer.Journal of the American Society for Mass Spectrometry · 2015Article
- Probing the electron capture dissociation mass spectrometry of phosphopeptides with traveling wave ion mobility spectrometry and molecular dynamics simulations.Journal of the American Society for Mass Spectrometry · 2015Article
- ECD of tyrosine phosphorylation in a triple quadrupole mass spectrometer with a radio-frequency-free electromagnetostatic cell.Journal of the American Society for Mass Spectrometry · 2014Article
- Imidate-based cross-linkers for structural proteomics: increased charge of protein and peptide ions and CID and ECD fragmentation studies.Journal of the American Society for Mass Spectrometry · 2014Article
- Using electron induced dissociation (EID) on an LC time-scale to characterize a mixture of analogous small organic molecules.Journal of the American Society for Mass Spectrometry · 2012Article
- Ultrasensitive identification of localization variants of modified peptides using ion mobility spectrometry.Analytical chemistry · 2011Article
- Metastable atom-activated dissociation mass spectrometry of phosphorylated and sulfonated peptides in negative ion mode.Journal of the American Society for Mass Spectrometry · 2011Article
- Dipole-guided electron capture causes abnormal dissociations of phosphorylated pentapeptides.Journal of the American Society for Mass Spectrometry · 2011Article
- Chemical arsenal for the study of O-GlcNAc.Molecules (Basel, Switzerland) · 2011Review
- Characterization of tyrosine nitration and cysteine nitrosylation modifications by metastable atom-activation dissociation mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011Article
- Separation of peptide isomers with variant modified sites by high-resolution differential ion mobility spectrometry.Analytical chemistry · 2010Article
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2 authors.
Funding
Abstract
The effect of site and frequency of phosphorylation on the electron capture dissociation of peptide ions has been investigated. The ECD of a suite of synthetic peptides (APLSFRGSLPKSYVK; one unmodified, three singly-phosphorylated, three-doubly phosphorylated, and one triply-phosphorylated); two tryptic phosphopeptides (YKVPQLEIVPN(p)SAEER, alpha-casein and FQ(p)SEEQQQTEDELQDK, beta-casein) and their unmodified counterparts, were determined over a range of ECD cathode potentials. The results show that, for doubly-charged precursor ions, the presence of phosphorylation has a deleterious effect on ECD sequence coverage. The fragmentation patterns observed suggest that for peptides with multiple basic residues, the phospho-groups exist in their deprotonated form and form salt-bridges with protonated amino acid side chains. The fragmentation observed for the acidic tryptic peptides suggested the presence of noncovalent interactions, which were perturbed on phosphorylation. Increasing the ECD electron energy significantly improves sequence coverage. Alternatively, improved sequence coverage can be achieved by performing ECD on triply-charged precursor ions. The findings are important for the understanding of gas-phase fragmentation of phosphopeptides.
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