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Identification of Protein Phosphorylation Sites by Advanced LC-ESI-MS/MS Methods

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Post-Translational Modification of Proteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1934))

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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Correspondence to Christof Lenz .

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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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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-4939-9053-5

  • Online ISBN: 978-1-4939-9055-9

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