构象异构
化学
对接(动物)
虚拟筛选
配体(生物化学)
背景(考古学)
计算化学
立体化学
分子动力学
生物化学
分子
医学
生物
古生物学
护理部
受体
有机化学
作者
Julian Tirado‐Rives,William L. Jorgensen
摘要
When a ligand binds to a protein, it is typically not in the lowest-energy conformation for the unbound ligand and there is also a loss of conformational degrees of freedom. The free-energy change for this "conformer focusing" is addressed here formally, and the associated errors with its estimation or neglect are considered in the context of scoring functions for protein−ligand docking and computation of absolute free energies of binding. Specific applications for inhibition of HIV-1 reverse transcriptase are reported. It is concluded that the uncertainties from this source alone are sufficient to preclude the viability of current docking methodology for rank-ordering of diverse compounds in high-throughput virtual screening.
科研通智能强力驱动
Strongly Powered by AbleSci AI