Premium
Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings
Author(s) -
Gronwald Wolfram,
Brunner Eike,
Huber Fritz,
Wenzler Michael,
Herrmann Christian,
Kalbitzer Hans Robert
Publication year - 2001
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.43201
Subject(s) - residual , dipole , residual dipolar coupling , spectral line , quality (philosophy) , physics , chemistry , chemical physics , biological system , computational chemistry , molecular physics , statistical physics , computer science , algorithm , biology , quantum mechanics
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.