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).
Similar content being viewed by others
References
Hirsch AKH, Fischer FR, Diederich F (2007) Angew Chem 119:342–357
Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S (2002) Science 298:1912–1934
McCauley TJ, Mathrubutham M, Morgan AG, Onken J, Stanaitis ML, Millis SZ (2004) J Assoc Lab Autom 9:171–176
Marino JP, Schwalbe H, Anklin C, Bermel W, Crothers DM, Griesinger C (1994) J Am Chem Soc 116:6472–6473
Berger S, Bast P (1993) Magn Reson Chem 31:1021–1023
Wagner R, Berger S (1996) J Magn Res Series A 120:258–260
Merrifield RB (1963) J Am Chem Soc 85:2149–2154
Pearson RB, Kemp BE (1991) Methods Enzymol 200:62–81
Daile P, Carnegie PR, Young JD (1975) Nature 257:416–418
Eylar EH, Brostoff S, Hashim G, Caccam J, Burnett P (1971) J Biol Chem 246:5770–5784
Acknowledgements
We are indebted to the research group of Dr Ralf Hoffmann, Leipzig, for invaluable help during peptide synthesis.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
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
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00216-007-1653-9