Phosphorylated amino acids: model compounds for solid-state 31P NMR spectroscopic studies of proteins.
Related Articles Phosphorylated amino acids: model compounds for solid-state 31P NMR spectroscopic studies of proteins.
Magn Reson Chem. 2004 Apr;42(4):369-72
Authors: Iuga A, Brunner E
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.
PMID: 15022197 [PubMed - indexed for MEDLINE]
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PubMed