Phosphorylated amino acids: model compounds for solid-state 31P NMR spectroscopic studies of proteins.
Solid-state 31P NMR spectroscopy was applied to measure the isotropic chemical shifts, chemical shift anisotropies and asymmetry parameters of three phosphorylated amino acids, O-phospho-L-serine, O-phospho-L-threonine and O-phospho-L-tyrosine. The cross-polarization buildup rates and longitudinal relaxation times of 31P and 1H were-determined and compared with the values measured for a triphosphate (GppCH2p) bound to a crystalline protein (Ras). It is shown that the phosphorylated amino acids are well-suited model compounds, e.g. for the optimization of experiments on crystalline proteins. Two-dimensional exchange experiments on O-phospho-L-tyrosine indicate the existence of an exchange between the two different conformations of the molecule.
Iuga
Adriana
A
Universität Regensburg, Institut für Biophysik und Physikalische Biochemie, D-93040 Regensburg, Germany.
Brunner
Eike
E
D000596:Amino Acids / Q000032:analysis* / Q000737:chemistry*; D003461:Crystallography / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009943:Organophosphorus Compounds / Q000032:analysis* / Q000737:chemistry*; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D011208:Powders; D011487:Protein Conformation
D000596:Amino Acids; D009943:Organophosphorus Compounds; D010761:Phosphorus Radioisotopes; D011208:Powders