Complexity and simplicity of ligand-macromolecule interactions: the energy landscape perspective.
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.
Verkhivker
Gennady M
GM
Department of Computational Chemistry, Agouron Pharmaceuticals Inc, A Pfizer Company, 10777 Science Center Drive, San Diego, California 92121-1111, USA. gennady.verkhivker@pfizer.com
Bouzida
Djamal
D
Gehlhaar
Daniel K
DK
Rejto
Paul A
PA
Freer
Stephan T
ST
Rose
Peter W
PW
D008024:Ligands; D046911:Macromolecular Substances; D008954:Models, Biological; D008958:Models, Molecular
D008024:Ligands; D046911:Macromolecular Substances