Post-translational modifications modulate the activity of most eukaryote proteins. Analysis of these modifications presents formidable challenges but their determination generates indispensable insight into biological function. Strategies developed to characterize individual proteins are now systematically applied to protein populations. The combination of function- or structure-based purification of modified 'subproteomes', such as phosphorylated proteins or modified membrane proteins, with mass spectrometry is proving particularly successful. To map modification sites in molecular detail, novel mass spectrometric peptide sequencing and analysis technologies hold tremendous potential. Finally, stable isotope labeling strategies in combination with mass spectrometry have been applied successfully to study the dynamics of modifications.
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We thank R. Zubarev, Uppsala University, for providing Figure 2. Work in the authors' laboratories is supported by a generous grant of the Danish National Research Foundation (M.M.) and the Danish Natural Sciences Research Council (O.N.J.) and infrastructure provided by the Danish Biotechnology Instrument Center(M.M. and O.N.J.).
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Mann, M., Jensen, O. Proteomic analysis of post-translational modifications. Nat Biotechnol 21, 255–261 (2003). https://doi.org/10.1038/nbt0303-255
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