Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings |
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| Authors: | Gronwald W Brunner E Huber F Wenzler M Herrmann C Kalbitzer H R |
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| Affiliation: | 1.Institut für Biophysik und physikalische Biochemie, Universität Regensburg, Postfach, D-93040 Regensburg, Federal Republic of Germany;2.Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, D-44227 Dortmund, Federal Republic of Germany |
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| 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 (1)H-(15)N 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. |
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| Keywords: | Byr2 residual dipolar couplings structure calculation NMR |
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