FREE-ENERGY OF CHARGES IN SOLVATED PROTEINS - MICROSCOPIC CALCULATIONS USING A REVERSIBLE CHARGING PROCESS
FREE-ENERGY OF CHARGES IN SOLVATED PROTEINS - MICROSCOPIC CALCULATIONS USING A REVERSIBLE CHARGING PROCESS
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DOI：
10.1021/bi00374a006
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发表时间：
1986-12-30
期刊：
影响因子：
2.9
通讯作者：
KING, G
中科院分区：
文献类型：
--
作者：
WARSHEL, A;SUSSMAN, F;KING, G
评价蛋白质中酸性基团的电离自由能可作为确定大分子中静电能计算可靠性的强有力的和一般的测试案例。这项工作的攻击这个测试用例，通过使用绝热充电过程中，评估与电离的酸性基团天冬氨酸-3和谷氨酸-7在牛胰蛋白酶抑制剂和天冬氨酸在溶液中的自由能的变化。这些自由能计算的结果是非常令人鼓舞的;这些自由能变化约为-70千卡/摩尔，误差范围约为1千卡/摩尔。这表明，我们终于接近获得定量结果的阶段，在建模溶剂化蛋白质的能量学。
Evaluation of the free energy of ionization of acidic groups in proteins may be used as a powerful and general test case for determining the reliability of calculations of electrostatic energies in macromolecules. This work attacks this test case by using an adiabatic charging process that evaluates the changes in free energies associated with ionizing the acidic groups Asp-3 and Glu-7 in bovine pancreatic trypsin inhibitor and aspartic acid in solution. The results of these free energy calculations are very encouraging; the error range is about 1 kcal/mol for these free energy changs of about -70 kcal/mol. This indicates that we are finally approaching the stage of obtaining quantitative results in modeling the energetics of solvated proteins.