Iuga, Adriana and Spoerner, Michael and Ader, Christian and Brunner, Eike and Kalbitzer, Hans Robert (2006) Rapid assignment of solution P-31 NMR spectra of large proteins by solid-state spectroscopy. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 346 (1). pp. 301-305. ISSN 0006-291X, 1090-2104
Full text not available from this repository. (Request a copy)Abstract
The application of the P-31 NMR spectroscopy to large proteins or protein complexes in solution is hampered by a relatively low intrinsic sensitivity coupled with large line widths. Therefore, the assignment of the phosphorus signals by two-dimensional NMR methods in solution is often extremely time consuming. In contrast, the quality of solid-state NMR spectra is not dependent on the molecular mass and the solubility of the protein. For the complex of Ras with the GTP-analogue GppCH(2)p we show solid-state P-31 NMR methods to be more sensitive by almost one order of magnitude than liquid-state NMR. Thus, solid-state NMR seems to be the method of choice for obtaining the resonance assignment of the phosphorus signals of protein complexes in solution. Experiments on Ras-GDP complexes show that the microcrystalline sample can be substituted by a precipitate of the sample and that unexpectedly the two structural states observed earlier in solution are present in crystals as well. (c) 2006 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | CONFORMATIONAL STATES; RAS PROTEIN; GTP ANALOG; HIGH-FIELD; C-13; COMPLEX; BINDING; DOMAIN; P-31 NMR; phosphate-binding proteins; solid-state NMR; liquid-state NMR; two-dimensional techniques |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Alumni or Retired > Prof. Dr. Eike Brunner Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 09 Feb 2021 14:56 |
| Last Modified: | 09 Feb 2021 14:56 |
| URI: | https://pred.uni-regensburg.de/id/eprint/34290 |
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