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dc.contributor.authorYang, JMen_US
dc.date.accessioned2014-12-08T15:41:30Z-
dc.date.available2014-12-08T15:41:30Z-
dc.date.issued2003en_US
dc.identifier.isbn3-540-40603-4en_US
dc.identifier.issn0302-9743en_US
dc.identifier.urihttp://hdl.handle.net/11536/28218-
dc.description.abstractWe have developed an evolutionary approach for the flexible docking that is now an important component of a rational drug design. This automatic docking tool, referred to as the GEMDOCK (Generic Evolutionary Method for DOCKing molecules), combines both global and local search strategies search mechanisms. GEMDOCK used a simple scoring function to recognize compounds by minimizing the energy of molecular interactions. The interactive types of atoms between ligands and proteins of our linear scoring function consist only hydrogen-bonding and steric terms. GEMDOCK has been tested on a diverse dataset of 100 protein-ligand complexes from Protein Data Bank. In total 76% of these complexes, it obtained docked ligand conformations with root mean square derivations (RMSD) to the crystal ligand structures less than 2.0 Angstrom when the ligand was docked back into the binding site. Experiments shows that the scoring function is simple and efficiently discriminates between native and non-native docked conformations. This study suggests that GEMDOCK is a useful tool for molecular recognition and is a potential docking tool for protein structure variations.en_US
dc.language.isoen_USen_US
dc.titleAn evolutionary approach for molecular dockingen_US
dc.typeArticle; Proceedings Paperen_US
dc.identifier.journalGENETIC AND EVOLUTIONARY COMPUTATION - GECCO 2003, PT II, PROCEEDINGSen_US
dc.citation.volume2724en_US
dc.citation.spage2372en_US
dc.citation.epage2383en_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.identifier.wosnumberWOS:000185074300129-
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