Abstract
Phosphorylation, the process by which a phosphate group is attached to a preexisting protein, is an evolutionarily and metabolically cheap way to change the protein’s surface and properties. It is presumably for that reason that it is the most widespread protein modification: An estimated 10–30% of all proteins are subject to phosphorylation.
MS-based methods are the methods of choice for the identification of phosphorylation sites; however biochemical pre-fractionation and enrichment protocols will be needed to produce suitable samples in the case of low-stoichiometry phosphorylation. Using emerging MS-based technology, the elucidation of the “phosphoproteome,” a comprehensive inventory of phosphorylation sites, will become a realistic goal. However, validating these findings in a cellular context and defining their biological meaning remains a daunting task, which will inevitably require extensive and time-consuming additional biological research.
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Lenz, C. (2019). Identification of Protein Phosphorylation Sites by Advanced LC-ESI-MS/MS Methods. In: Kannicht, C. (eds) Post-Translational Modification of Proteins. Methods in Molecular Biology, vol 1934. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9055-9_11
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DOI: https://doi.org/10.1007/978-1-4939-9055-9_11
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