Calculation of the relative change in binding free energy of a protein-inhibitor complex. Export

@article{citeulike:2267576, abstract = {By means of a thermodynamic perturbation method implemented with molecular dynamics, the relative free energy of binding was calculated for the enzyme thermolysin complexed with a pair of phosphonamidate and phosphonate ester inhibitors. The calculated difference in free energy of binding was 4.21 +/- 0.54 kilocalories per mole. This compares well with the experimental value of 4.1 kilocalories per mole. The method is general and can be used to determine a change or "mutation" in any system that can be suitably represented. It is likely to prove useful for protein and drug design.}, author = {Bash, P. A. and Singh, U. C. and Brown, F. K. and Langridge, R. and Kollman, P. A.}, citeulike-article-id = {2267576}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.3810157}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/235/4788/574}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/3810157}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=3810157}, day = {30}, doi = {10.1126/science.3810157}, issn = {0036-8075}, journal = {Science}, keywords = {energy, free}, month = {January}, number = {4788}, pages = {574--576}, posted-at = {2008-01-21 12:01:15}, priority = {2}, title = {Calculation of the relative change in binding free energy of a protein-inhibitor complex.}, url = {http://dx.doi.org/10.1126/science.3810157}, volume = {235}, year = {1987} }

TY - JOUR ID - citeulike:2267576 L3 - citeulike-article-id:2267576 N2 - By means of a thermodynamic perturbation method implemented with molecular dynamics, the relative free energy of binding was calculated for the enzyme thermolysin complexed with a pair of phosphonamidate and phosphonate ester inhibitors. The calculated difference in free energy of binding was 4.21 +/- 0.54 kilocalories per mole. This compares well with the experimental value of 4.1 kilocalories per mole. The method is general and can be used to determine a change or "mutation" in any system that can be suitably represented. It is likely to prove useful for protein and drug design. IS - 4788 JF - Science SN - 0036-8075 EP - 576 TI - Calculation of the relative change in binding free energy of a protein-inhibitor complex. VL - 235 SP - 574 KW - energy KW - free AU - Bash, PA AU - Singh, UC AU - Brown, FK AU - Langridge, R AU - Kollman, PA PY - 1987/01/30/ UR - http://dx.doi.org/10.1126/science.3810157 ER -