Estimation of binding free energies for HIV proteinase inhibitors by molecular dynamics simulations
Estimation of binding free energies for HIV proteinase inhibitors by molecular dynamics simulations
复制标题
DOI：
10.1093/protein/8.11.1137
复制
发表时间：
1995-11-01
期刊：
影响因子：
--
通讯作者：
Aqvist, J
中科院分区：
文献类型：
--
作者：
Hansson, T;Aqvist, J
本文用线性近似法从分子动力学模拟中估算了三种HIV-1蛋白酶抑制剂的绝对结合自由能。结果与实验结合数据相当吻合。两个抑制剂是非常相似的，为了比较，他们的相对自由能的结合也计算自由能微扰法，得到几乎相同的结果。的截止半径和蛋白质模型的电荷状态的影响进行了检查。预测了pH对其中一种抑制剂结合的影响。
Absolute binding free energies for three inhibitors of HIV-1 proteinase were estimated from molecular dynamics simulations by a recently reported linear approximation procedure. The results were in fairly good agreement,vith experimental binding data. Two of the inhibitors were very similar and, for comparison, their relative free energies of binding were also calculated by free energy perturbation methods, giving virtually the same result. Effects of cutoff radii and charge states of the protein model were examined. The effects of pH on binding of one of the inhibitors were predicted.