期刊
JOURNAL OF PROTEOME RESEARCH
卷 8, 期 6, 页码 2633-2639出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr800834e
关键词
ETD; fragmentation mechanism; phosphopeptide; supplemental activation; directed proteomics
资金
- ETH Zurich
- Swiss National Science Foundation [31000-10767]
- F Hoffmann-La Roche, Ltd. (Basel, Switzerland)
- Competence Center for Systems Physiology and Metabolic Disease
Better understanding how cells are regulated and adapt to their environment based on the reversible phosphorylation of proteins is a key question of current molecular and systems biology research. In this study, an advanced mass spectrometry based approach leveraging the electron transfer dissociation (ETD) technique in combination with CID using a linear ion trap mass spectrometer is described. The technique was applied, for the first time, to the identification of phosphorylated peptides isolated from the Drosophila melanogaster Kc167 cell line. We demonstrate that the method is particularly useful for the characterization of large phosphopeptides, including those with multiple phosphorylation sites, as extensive series of c' and z* fragment-ions were observed. Finally, we have applied a directed tandem mass spectrometric workflow using inclusion lists to increase the number of identified peptides.
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