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A 2D NMR method to study peptide phosphorylation

Analytical and Bioanalytical Chemistry volume 389, pages 2161–2165 (2007)Cite this article

Abstract

We demonstrate a 2D NMR method which distinguishes between phosphorylated and non-phosphorylated amino acids. The method is capable of monitoring the amino acid and site-specific enzymatic phosphorylation and dephosphorylation of peptides. The method was developed using O-phosphorylated amino acids and its potential is shown with a peptide fragment of the myelin basic protein (MBP).

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Acknowledgements

We are indebted to the research group of Dr Ralf Hoffmann, Leipzig, for invaluable help during peptide synthesis.

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Affiliations

  1. Institute of Analytical Chemistry, University of Leipzig, Linnéstr. 3, Leipzig, 04103, Germany

    Christian Raeck & Stefan Berger

Authors
  1. Christian Raeck
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  2. Stefan Berger
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Correspondence to Stefan Berger.

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Raeck, C., Berger, S. A 2D NMR method to study peptide phosphorylation. Anal Bioanal Chem 389, 2161–2165 (2007). https://doi.org/10.1007/s00216-007-1653-9

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  • DOI: https://doi.org/10.1007/s00216-007-1653-9

Keywords

  • Phosphorylation
  • NMR
  • Peptides
  • Kinase
  • Phosphatase