Iuga, Adriana and Brunner, Eike (2004) Phosphorylated amino acids: model compounds for solid-state P-31 NMR spectroscopic studies of proteins. MAGNETIC RESONANCE IN CHEMISTRY, 42 (4). pp. 369-372. ISSN 0749-1581, 1097-458X
Full text not available from this repository. (Request a copy)Abstract
Solid-state P-31 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 P-31 and H-1 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 (C) 2004 John Wiley Sons, Ltd.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | NUCLEAR-MAGNETIC-RESONANCE; ROTATING SOLIDS; DILUTE SPINS; C-13; PHOSPHATES; TYROSINE; EXCHANGE; SYSTEMS; SPECTRA; COMPLEX; NMR; H-1 NMR; P-31 NMR; solid-state P-31 NMR; cross-polarization; magic angle spinning; relaxation; conformational exchange; phosphorylated amino acids; proteins |
| Subjects: | 500 Science > 530 Physics 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Alumni or Retired > Prof. Dr. Eike Brunner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 21 Jul 2021 09:24 |
| Last Modified: | 21 Jul 2021 09:24 |
| URI: | https://pred.uni-regensburg.de/id/eprint/37825 |
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