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- W78060306 abstract "Biomarker discovery relies heavily on DNA data bases to identify biomarker candidates. However, such data bases reveal nothing about the post-translation modifications (PTMs) that decorate a protein or peptide and contribute to their essential activity. Characterizing these modifications is a requirement for subsequent validation studies.The most prevalent PTM is phosphorylation which impacts more than one third of all proteins in a cell. For biomarker studies that focus on secreted proteins, glycosylation is a universal characteristic of such proteins. For biomarker studies looking at the peptidome many of these peptides have a disulfide bridge that constrains the peptide in a particular shape.Although mass spectrometry (MS) with collisional-induced-dissociation (CID) of peptides has proven to be a powerful and sensitive technique for the identification of candidate biomarkers, it has limitations in mapping PTM sites because the PTM attachment to the specific amino acid residue is often lost. This is not the case with a new dissociation technique referred to as Electron Transfer Dissociation (ETD). ETD cleaves the peptide backbone, but unlike (CID) it leaves phosphoryl groups attached to their amino acid sites.This works presents the application of ETD to the characterization of PTM sites. The application of alternating MS scans with CID followed by ETD on an LC time scale will be shown for the elucidation of PTM sites." @default.
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- W78060306 date "2007-02-01" @default.
- W78060306 modified "2023-09-24" @default.
- W78060306 title "P115-S Mapping PTMs with Electron Transfer Dissociation" @default.
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