CALCULATION OF THE RELATIVE CHANGE IN BINDING FREE-ENERGY OF A PROTEIN-INHIBITOR COMPLEX
CALCULATION OF THE RELATIVE CHANGE IN BINDING FREE-ENERGY OF A PROTEIN-INHIBITOR COMPLEX
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DOI：
10.1126/science.3810157
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发表时间：
1987-01-30
期刊：
影响因子：
56.9
通讯作者：
KOLLMAN, PA
中科院分区：
文献类型：
--
作者：
BASH, PA;SINGH, UC;KOLLMAN, PA
通过分子动力学实施的热力学微扰方法，计算了与一对膦酰胺和膦酸酯抑制剂复合的嗜热菌蛋白酶的相对结合自由能。计算出的结合自由能差为4.21±。每摩尔 0.54 卡路里。这与每摩尔 4.1 千卡的实验值相吻合。该方法是通用的，可以用来确定任何可以适当表示的系统中的变化或“突变”。它可能对蛋白质和药物设计有用。
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.