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Nature Biotechnology
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Proteomic analysis of post-translational modifications

Nature Biotechnologyvolume 21, pages255–261 (2003)Cite this article

Abstract

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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Figure 1: Strategy for mapping post-translational modifications.
Figure 2: Determination of a glycosylation site by FTMS and ECD.
Figure 3: Analysis of the phosphoproteome.

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Acknowledgements

We thank R. Zubarev, Uppsala University, for providingFigure 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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Authors and Affiliations

  1. Center for Experimental BioInformatics (CEBI) Department of Biochemistry and Molecular Biology, Center for Experimental BioInformatics (CEBI), University of Southern Denmark, Campusvej 55, Odense M, DK-5230, Denmark

    Matthias Mann

  2. Department of Biochemistry Molecular Biology, Protein Research Group, University of Southern Denmark, Campusvej 55, Odense M, DK-5230, Denmark

    Ole N. Jensen

Authors
  1. Matthias Mann
  2. Ole N. Jensen

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Mann, M., Jensen, O. Proteomic analysis of post-translational modifications.Nat Biotechnol21, 255–261 (2003). https://doi.org/10.1038/nbt0303-255

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