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Phosphorylated amino acids: model compounds for solid‐state 31 P NMR spectroscopic studies of proteins
Author(s) -
Iuga Adriana,
Brunner Eike
Publication year - 2004
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1356
Subject(s) - chemistry , serine , nuclear magnetic resonance spectroscopy , tyrosine , amino acid , threonine , solid state nuclear magnetic resonance , chemical shift , molecule , phosphorylation , anisotropy , spectroscopy , crystallography , stereochemistry , organic chemistry , biochemistry , nuclear magnetic resonance , physics , quantum mechanics
Solid‐state 31 P 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 31 P and 1 H were‐determined and compared with the values measured for a triphosphate (GppCH 2 p) 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. Copyright © 2004 John Wiley & Sons, Ltd.