Ontology highlight
ABSTRACT:
SUBMITTER: Orts J
PROVIDER: S-EPMC3266494 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
Journal of biomolecular NMR 20111214 1
Low-affinity ligands can be efficiently optimized into high-affinity drug leads by structure based drug design when atomic-resolution structural information on the protein/ligand complexes is available. In this work we show that the use of a few, easily obtainable, experimental restraints improves the accuracy of the docking experiments by two orders of magnitude. The experimental data are measured in nuclear magnetic resonance spectra and consist of protein-mediated NOEs between two competitive ...[more]