title: Complexity and simplicity of ligand-macromolecule interactions: the energy landscape perspective.
abstract: The energy landscape approach has contributed to recent progress in understanding the complexity and simplicity of ligand-macromolecule interactions. Significant advances in computational structure prediction of ligand-protein complexes have been made using approaches that include the effects of protein flexibility and incorporate a hierarchy of energy functions. The results suggest that the complexity of structure prediction in molecular recognition may be determined by low-resolution properties of the underlying binding energy landscapes and by the nature of the energy funnels near the native structures of the complexes.
authors.affiliation: Department of Computational Chemistry, Agouron Pharmaceuticals Inc, A Pfizer Company, 10777 Science Center Drive, San Diego, California 92121-1111, USA. gennady.verkhivker@pfizer.com
authors.forename: Gennady M
authors.initials: GM
authors.lastname: Verkhivker
authors.forename: Djamal
authors.initials: D
authors.lastname: Bouzida
authors.forename: Daniel K
authors.initials: DK
authors.lastname: Gehlhaar
authors.forename: Paul A
authors.initials: PA
authors.lastname: Rejto
authors.forename: Stephan T
authors.initials: ST
authors.lastname: Freer
authors.forename: Peter W
authors.initials: PW
authors.lastname: Rose
mesh_terms: D008024:Ligands; D046911:Macromolecular Substances; D008954:Models, Biological; D008958:Models, Molecular
chemical_list: D008024:Ligands; D046911:Macromolecular Substances