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Mapping of phosphorylation sites by LC-MS/MS.
Journal article

Mapping of phosphorylation sites by LC-MS/MS.

  • Gerrits B Functional Genomics Center Zurich, University of Zurich and Swiss Federal Institute of Technology, Zurich, Switzerland.
  • Bodenmiller B
  • 2010-09-15
Published in:
  • Methods in molecular biology (Clifton, N.J.). - 2010
Analytic Sample Preparation Methods
Binding Sites
Chromatography, Affinity
Chromatography, Liquid
Databases, Protein
Dendrimers
Microspheres
Organophosphorus Compounds
Peptide Fragments
Phosphoproteins
Phosphorylation
Proteins
Tandem Mass Spectrometry
Titanium
English Reversible protein phosphorylation ranks among the most important post-translational modifications that occurs in the cell. It is therefore highly relevant to elucidate the phosphorylation states of a given biological system, albeit challenging. Most notably the often low stoichiometry of phosphorylation is inherently incompatible with standard LC-MS analysis of a complex protein digest mixture, primarily due to the relative low dynamic range of current mass analyzers. Therefore a need for specific enrichment of phosphorylated peptides or proteins exists. Significant progress surrounding the biochemical analysis of reversible protein phosphorylation in the past years has led to the development of several new techniques to isolate or enrich phosphopeptides, particularly in large-scale analyses. This chapter deals with three such examples.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://roar.hep-bejune.ch/global/documents/153306
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