Rapid classification of a protein fold family using a statistical analysis of dipolar couplings.
BACKGROUND
One of the primary aims of the structural genomics initiative is the determination of representative structures from each protein fold family. Given this objective, it is important to rapidly identify proteins that belong to a family that is already well populated (so they can be eliminated from further studies), or more importantly identify proteins that represent new families of fold.


RESULTS
A method for rapid classification to a fold family by the statistical analyses of unassigned the (15)N-(1)H residual dipolar couplings is presented. The required NMR data can be quickly acquired and analyzed. Using this method, structure determination efforts can be focused on more unique and interesting structures, and the overall efficiency in the construction of an information-rich library can be increased.
Valafar
Homayoun
H
Southeast Collaboratory for Structural Genomics Complex Carbohydrate Research Center, University of Georgia, 220 Riverbend Road, Athens, GA 30602, USA.
Prestegard
James H
JH
D000465:Algorithms; D003198:Computer Simulation; D030562:Databases, Protein; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000145:classification*; D021281:Quantitative Structure-Activity Relationship; D016415:Sequence Alignment / Q000379:methods*; D020539:Sequence Analysis, Protein / Q000379:methods*
D011506:Proteins