Paper Info
Title
Refinement of NMR-determined protein structures with database derived distance constraints.
Abstract
The protein structures determined by NMR (Nuclear Magnetic Resonance Spectroscopy) are not as detailed and accurate as those by X-ray crystallography and are often underdetermined due to the inadequate distance data available from NMR experiments. The uses of NMR-determined structures in such important applications as homology modeling and rational drug design have thus been severely limited. Here we show that with the increasing numbers of high quality protein structures being determined, a computational approach to enhancing the accuracy of the NMR-determined structures becomes possible by deriving additional distance constraints from the distributions of the distances in databases of known protein structures. We show through a survey on 462 NMR structures that, in fact, many inter-atomic distances in these structures deviate considerably from their database distributions and based on the refinement results on 10 selected NMR structures that these structures can actually be improved significantly when a selected set of distances are constrained within their high probability ranges in their database distributions.
Year
DOI
Venue
2005
10.1142/S0219720005001582
J. Bioinformatics and Computational Biology
Keywords
Field
DocType
structural bioinformatics.,nmr protein structure refinement,protein structure database,homology modeling,x ray crystallography,structural bioinformatics,nuclear magnetic resonance spectroscopy,rational drug design,protein structure
Structural bioinformatics,Protein structure database,Underdetermined system,Drug design,Chemistry,Bioinformatics,Homology modeling,Database,Nuclear magnetic resonance spectroscopy,Protein structure
Journal
Volume
Issue
ISSN
3
6
0219-7200
Citations 
PageRank 
References 
8
2.21
1
Authors
3
Name
Order
Citations
PageRank
Feng Cui1176.44
Robert L Jernigan222425.36
Zhijun Wu36612.32