Protein phosphorylation analysis by mass spectrometry
Part 3. Proteomics
3.5. Proteome Diversity
Published Online: 15 APR 2005
Copyright © 2005 John Wiley & Sons, Ltd
Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics
How to Cite
Steen, H. and Jebanathirajah, J. A. 2005. Protein phosphorylation analysis by mass spectrometry. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics. 3:3.5:63.
- Published Online: 15 APR 2005
Phosphorylation is arguably the most important posttranslational protein modification, being heavily involved in the dynamic regulation of protein function during signaling, proliferation, and differentiation. Localizing and quantitating the sites of phosphorylation on proteins is of paramount importance toward understanding the regulation of proteins by phosphorylation. Although biochemical methods in combination with methods based on the detection of the radioactive phosphorus isotopes 32P and 33P are still used, radioactive-free methods utilizing mass spectrometry are becoming widespread because of its speed, sensitivity, and the ability to handle complex protein and peptide mixtures. This review summarizes recent and established methods used for the selective enrichment, derivatization, and selective mass spectrometric detection of phosphorylated species, which have proven to be extremely useful in numerous studies. In addition, the latest trends in the field of mass spectrometric analysis of protein phosphorylation are introduced.
- mass spectrometry;
- precursor ion scanning;
- neutral loss scanning;
- peptide fragmentation;