Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings

Citation
W. Gronwald et al., Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings, PROTEIN SCI, 10(6), 2001, pp. 1260-1263
Citations number
15
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEIN SCIENCE
ISSN journal
0961-8368 → ACNP
Volume
10
Issue
6
Year of publication
2001
Pages
1260 - 1263
Database
ISI
SICI code
0961-8368(200106)10:6<1260:OTPAWP>2.0.ZU;2-U
Abstract
For the Ras-binding domain of the protein kinase Byr2, only a limited numbe r 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 d ipolar couplings in the beginning of the structure determination process al lows to overcome this problem. We used a three-step recipe for this procedu re. A previously unknown structure could be calculated reasonably well with only a limited number of unambiguously assigned NOE contacts.