Gronwald, W. and Brunner, E. and Huber, F. and Wenzler, M. and Herrmann, C. 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.
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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.
|Institutions:||Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer|
|Subjects:||500 Science > 570 Life sciences|
|Created at the University of Regensburg:||Unknown|
|Deposited On:||15 Sep 2010 11:06|
|Last Modified:||15 Sep 2010 11:06|
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