Complexity and simplicity of ligand–macromolecule interactions: the energy landscape perspective Export

@article{citeulike:4173290, 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.}, author = {Verkhivker, G.}, citeulike-article-id = {4173290}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0959-440X(02)00310-X}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0959-440X(02)00310-X}, day = {1}, doi = {10.1016/S0959-440X(02)00310-X}, issn = {0959440X}, journal = {Current Opinion in Structural Biology}, keywords = {free\_energy}, month = {April}, number = {2}, pages = {197--203}, posted-at = {2009-03-14 10:26:30}, priority = {2}, title = {Complexity and simplicity of ligand–macromolecule interactions: the energy landscape perspective}, url = {http://dx.doi.org/10.1016/S0959-440X(02)00310-X}, volume = {12}, year = {2002} }

TY - JOUR ID - citeulike:4173290 L3 - citeulike-article-id:4173290 N2 - 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. IS - 2 JF - Current Opinion in Structural Biology SN - 0959440X EP - 203 TI - Complexity and simplicity of ligand–macromolecule interactions: the energy landscape perspective VL - 12 SP - 197 KW - free_energy AU - Verkhivker, G PY - 2002/04/01/ UR - http://dx.doi.org/10.1016/S0959-440X(02)00310-X ER -