@article{bibcite_193,
  keywords = {Humans, Aspartic Acid Endopeptidases, HIV-1, Static Electricity, Enzyme Inhibitors, Cyclin-Dependent Kinase 2, Quantum Theory, RNA Helicases, Serine Endopeptidases, Viral Nonstructural Proteins, West Nile virus},
  author = {T. Zhou and D. Huang and A. Caflisch},
  title = {Is quantum mechanics necessary for predicting binding free energy?},
  abstract = {<p>To take into account polarization effects, the linear interaction energy model with continuum electrostatic solvation (LIECE) is supplemented by the linear-scaling semiempirical quantum mechanical calculation of the intermolecular electrostatic energy (QMLIECE). QMLIECE and LIECE are compared on three enzymes belonging to different classes: the West Nile virus NS3 serine protease (WNV PR), the aspartic protease of the human immunodeficiency virus (HIV-1 PR), and the human cyclin-dependent kinase 2 (CDK2). QMLIECE is superior for 44 peptidic inhibitors of WNV PR because of the different amount of polarization due to the broad range of formal charges of the inhibitors (from 0 to 3). On the other hand, QMLIECE and LIECE show similar accuracy for 24 peptidic inhibitors of HIV-1 PR (20 neutral and 4 with one formal charge) and for 73 CDK2 inhibitors (all neutral). These results indicate that quantum mechanics is essential when the inhibitor/protein complexes have highly variable charge-charge interactions.</p>},
  year = {2008},
  journal = {Journal of Medicinal Chemistry},
  volume = {51},
  pages = {4280-4288},
  month = {2008 Jul 24},
  issn = {1520-4804},
  doi = {10.1021/jm800242q},
  language = {eng},
}