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Electron transfer dissociation in conjunction with collision activation to investigate the Drosophila melanogaster phosphoproteome.
Journal article

Electron transfer dissociation in conjunction with collision activation to investigate the Drosophila melanogaster phosphoproteome.

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  • 2009-05-14
Published in:
  • Journal of proteome research. - 2009
Amino Acid Sequence
Animals
Cell Line
Chromatography, Liquid
Drosophila Proteins
Drosophila melanogaster
Molecular Sequence Data
Peptides
Phosphopeptides
Phosphoproteins
Phosphorylation
Proteome
Proteomics
Tandem Mass Spectrometry
English 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/47315
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