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What Interest Mass Spectrometry Provides in the Determination and Quantification of Post-Translational Modifications?

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Mass Spectrometry: Developmental Approaches to Answer Biological Questions

Part of the book series: SpringerBriefs in Bioengineering ((BRIEFSBIOENG))

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Abstract

Post-translational modifications (PTM) of proteins play a pivotal role in the function and the structure of proteins. It exists hundreds of modifications that are known and studied. Mass spectrometry is one of the methods used for the identification and the characterization of PTM. With the information provided by this technique it is possible to determine the type of modification, its structure and its position in the protein sequence. Those informations are crucial for the influence of the PTM on the proteins. The current chapter presents mass spectrometry methods involved in the analysis of post-translational modifications. It highlights as well some technical caveats linked to the chemistry of the modifications and the dissociation method employed. Then, the conditions of preparation and the methods of measurement depend on the PTM investigated.

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  1. PDRA, Pharmacology Department, University of Oxford, Oxford, United Kingdom

    Gwenael Pottiez

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  1. Gwenael Pottiez
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Correspondence to Gwenael Pottiez .

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Pottiez, G. (2015). What Interest Mass Spectrometry Provides in the Determination and Quantification of Post-Translational Modifications?. In: Mass Spectrometry: Developmental Approaches to Answer Biological Questions. SpringerBriefs in Bioengineering. Springer, Cham. https://doi.org/10.1007/978-3-319-13087-3_5

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