Gronwald, Wolfram and Brunner, Eike and Huber, Fritz and Wenzler, Michael and Herrmann, Christian and Kalbitzer, Hans Robert (2001) Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings. PROTEIN SCIENCE, 10 (6). pp. 1260-1263. ISSN 0961-8368
Full text not available from this repository. (Request a copy)Abstract
For the Ras-binding domain of the protein kinase Byr2, only a limited number of NOE contacts could be initially assigned unambiguously, as the quality of the NOESY spectra was too poor. However, the use of residual H-1-N-15 dipolar couplings in the beginning of the structure determination process allows to overcome this problem. We used a three-step recipe for this procedure. A previously unknown structure could be calculated reasonably well with only a limited number of unambiguously assigned NOE contacts.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | RAS-BINDING DOMAIN; NMR; MACROMOLECULES; Byr2; residual dipolar couplings; structure calculation; NMR |
| 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: | 25 Jan 2022 08:05 |
| Last Modified: | 25 Jan 2022 08:05 |
| URI: | https://pred.uni-regensburg.de/id/eprint/41416 |
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