A 2D NMR method to study peptide phosphorylation.
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).
Raeck
Christian
C
Institute of Analytical Chemistry, University of Leipzig, Linnéstr. 3, Leipzig, 04103, Germany.
Berger
Stefan
S
D000596:Amino Acids / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D015394:Molecular Structure; D010455:Peptides / Q000032:analysis / Q000737:chemistry*; D010766:Phosphorylation
D000596:Amino Acids; D010455:Peptides