Protein ADP-ribosylation is a post-translational modification involved in important physiological and pathological processes. Here, we present an optimized method using the Orbitrap Fusion Tribrid mass spectrometer, which drastically improves the overall ADP-ribosylation site localization score and boosts the identification of ADP-ribosylated peptides. We compared the HCD, ETcaD or EThcD fragmentation methods for the identification of ADP-ribose acceptor sites in a complex cellular sample and further combined them in a product dependent manner, exploiting the unique fragmentation properties of the ADP-ribose moiety as a trigger for a targeted fragmentation of modified peptides.
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: ADP-ribosylome ; EThcD ; HCD ; Product dependent method
Principal Investigators: (in alphabetical order) |
Prof. Michael O.Hottiger |
Submitting User: | verabilan |
Bilan V, Leutert M, Nanni P, Panse C, Hottiger MO.
Combining Higher-Energy Collision Dissociation and Electron-Transfer/Higher-Energy Collision Dissociation Fragmentation in a Product-Dependent Manner Confidently Assigns Proteomewide ADP-Ribose Acceptor Sites.
Anal. Chem. 2017 Feb 7;89(3):1523-1530. Epub 2017 Jan 13.
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