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P102-T Electron Transfer Dissociation, Multi-Stage Activation, and Neutral Loss Initiated MS3 Utilized in the Characterization of Phosphorylation Sites of Human Kinases

By M. P. Hornshaw and N. Morrice

Abstract

The standard mass spectrometric technique for the analysis of phosphopeptides on a linear ion trap mass spectrometer is to perform MS/MS followed by MS3 of the putative neutral loss peak observed by MS/MS. This is usually termed data-dependent neutral loss MS3 (DDN-LMS3). The strength of this approach is the sensitivity in full scan MSn of linear ion trap technology and the characteristically strong neutral loss peak, which flags the MS/ MS spectrum as potentially belonging to a phosphopeptide. This approach has been much applied to phospho-proteomic analyses typically involving up-front phosphopeptide enrichment, such as TiO2 chromatography. Indeed, a recent article from Mann and co-workers identified 6600 phosphorylation sites utilizing a hybrid linear ion trap Fourier transform mass spectrometer. However, there are also weaknesses, such as the fact that phosphotyrosine residues rarely produce a neutral loss from the precursor during MS/MS

Topics: Poster Abstracts: Mass Spectrometry
Publisher: The Association of Biomolecular Resource Facilities
OAI identifier: oai:pubmedcentral.nih.gov:2291950
Provided by: PubMed Central
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