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- W2899866399 abstract "Free radical–initiated peptide sequencing mass spectrometry (FRIPS MS) was employed to analyze a number of representative singly or doubly protonated phosphopeptides (phosphoserine and phosphotyrosine peptides) in positive ion mode. In contrast to collision-activated dissociation (CAD) results, a loss of a phosphate group occurred to a limited degree for both phosphoserine and phosphotyrosine peptides, and thus, localization of a phosphorylated site was readily achieved. Considering that FRIPS MS supplies a substantial amount of collisional energy to peptides, this result was quite unexpected because a labile phosphate group was conserved. Analysis of the resulting peptide fragments revealed the extensive production of a-, c-, x-, and z-type fragments (with some minor b- and y-type fragments), suggesting that radical-driven peptide fragmentation was the primary mechanism involved in the FRIPS MS of phosphopeptides. Results of this study clearly indicate that FRIPS MS is a promising tool for the characterization of post-translational modifications such as phosphorylation." @default.
- W2899866399 created "2018-11-16" @default.
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- W2899866399 date "2018-11-09" @default.
- W2899866399 modified "2023-09-26" @default.
- W2899866399 title "Free Radical–Initiated Peptide Sequencing Mass Spectrometry for Phosphopeptide Post-translational Modification Analysis" @default.
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- W2899866399 doi "https://doi.org/10.1007/s13361-018-2100-1" @default.
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