Wang C X, Shi Y Y, Zhou F, Wang L
Center for Fundamental Physics, University of Science and Technology of China, Hefei.
Proteins. 1993 Jan;15(1):5-9. doi: 10.1002/prot.340150103.
The binding free energy difference for the Gly-169-->Ala-169 (G169A) mutation in subtilism BPN' complexed with a tripeptide substrate analogue is explored using the thermodynamic integration approach. The structure of the mutant enzyme-substrate complex obtained from free energy simulation is in good agreement with experimental X-ray refinement. The near perfect reversibility is obtained in the present work for ensuring the correctness of the free energy calculations. The results of the binding free energy difference are close to similar experimental data.
采用热力学积分方法探究了枯草杆菌蛋白酶BPN'与三肽底物类似物复合时Gly-169→Ala-169（G169A）突变的结合自由能差异。通过自由能模拟得到的突变酶-底物复合物结构与实验X射线精修结果高度吻合。在本工作中获得了近乎完美的可逆性以确保自由能计算的正确性。结合自由能差异的结果与类似实验数据相近。
