17. Quantification of Post-Translational Modifications

  1. Ingvar Eidhammer,
  2. Harald Barsnes,
  3. Geir Egil Eide and
  4. Lennart Martens

Published Online: 10 JAN 2013

DOI: 10.1002/9781118494042.ch17

Computational and Statistical Methods for Protein Quantification by Mass Spectrometry

Computational and Statistical Methods for Protein Quantification by Mass Spectrometry

How to Cite

Eidhammer, I., Barsnes, H., Eide, G. E. and Martens, L. (2013) Quantification of Post-Translational Modifications, in Computational and Statistical Methods for Protein Quantification by Mass Spectrometry, John Wiley & Sons Ltd, Oxford, UK. doi: 10.1002/9781118494042.ch17

Publication History

  1. Published Online: 10 JAN 2013
  2. Published Print: 4 JAN 2013

ISBN Information

Print ISBN: 9781119964001

Online ISBN: 9781118494042

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Keywords:

  • absolute modification degrees;
  • discovery based modification stoichiometry;
  • mass spectrometry;
  • post-translational modifications (PTMs);
  • relative modification degree

Summary

Post-translational modifications (PTMs) are crucial for the heterogeneity of proteins. PTMs are often used to regulate how proteins will act in eukaryotic organisms; disregulation of PTMs is important in many diseases. Examining how the extent of modifications varies over different situations is therefore interesting from both a basic biological as well as from a clinical perspective. Although mass spectrometry has been applied to the quantification of PTMs for more than ten years, there are essentially no general methods available that can analyze all types of modifications. Absolute modification degrees have to be calculated from the observed abundances. Relative modification degree can be calculated from absolute modification degrees. The chapter also discusses discovery based modification stoichiometry.

Controlled Vocabulary Terms

Computational statistics Inferential statistics