@article{bibcite_96,
  keywords = {Models, Molecular, Thermodynamics, HIV Protease Inhibitors, Protein Binding, Amyloid Precursor Protein Secretases, Endopeptidases, HIV Protease, Protease Inhibitors, Static Electricity},
  author = {D. Huang and A. Caflisch},
  title = {Efficient evaluation of binding free energy using continuum electrostatics solvation},
  abstract = {<p>The linear interaction energy (LIE) method is combined with energy minimization and finite-difference Poisson calculation of electrostatic solvation for the estimation of the absolute free energy of binding. A predictive accuracy of about 1.0 kcal/mol is obtained for 13 and 29 inhibitors of \&beta;-secretase (BACE) and HIV-1 protease (HIV-1 PR), respectively. The multiplicative coefficients for the van der Waals and electrostatic terms are not transferable between BACE and HIV-1 PR although they are both aspartic proteases. The present approach is about 2 orders of magnitude faster than previous LIE methods and can be used for ranking large libraries of structurally diverse compounds docked by automatic computational tools.</p>},
  year = {2004},
  journal = {Journal of Medicinal Chemistry},
  volume = {47},
  pages = {5791-5797},
  month = {2004 Nov 4},
  issn = {0022-2623},
  doi = {10.1021/jm049726m},
  language = {eng},
}