| Literature DB >> 19965178 |
Yue Shi1, Dian Jiao, Michael J Schnieders, Pengyu Ren.
Abstract
The binding free energies of several benzamidine -like inhibitors to trypsin were examined using a polarizable molecular mechanics potential. All the computed binding free energies are in good agreement with the experimental data. From free energy decomposition, electrostatic interaction was indicated to be the driving force for the binding. MD simulations show that the ligands form hydrogen bonds with trypsin and water molecules nearby in a competitive fashion. While the binding free energy is independent of the ligand dipole moment, it shows a strong correlation with the ligand molecular polarizability.Entities:
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Year: 2009 PMID： 19965178 PMCID： PMC2819397 DOI： 10.1109/IEMBS.2009.5335108
Source DB: PubMed Journal: Conf Proc IEEE Eng Med Biol Soc ISSN： 1557-170X