Thermodynamics of amide hydrogen bond formation in polar and apolar solvents.
Thermodynamics of amide hydrogen bond formation in polar and apolar solvents.
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DOI：
10.1016/0022-2836(89)90609-8
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发表时间：
1989-10
影响因子：
5.6
通讯作者：
S. Sneddon;D. Tobias;C. Brooks
中科院分区：
文献类型：
--
作者：
S. Sneddon;D. Tobias;C. Brooks
我们提出了水和四氯化碳中两个甲酰胺分子之间氢键形成的理论研究的初步结果。这些系统被选为蛋白质表面附近的极性环境和蛋白质内部的非极性环境中二级结构形成的最简单模型。我们采用热力学模拟方法来获得两种溶剂中肽氢键形成的绝对结合自由能和自由能分布。我们发现酰胺氢键在CCl4 中稳定8·4 kcal/mol，在水中稳定0·3 kcal/mol。我们的结果还表明，氢键二聚体在水中比在 CCl4 中稳定 2·2 kcal/mol。我们将我们的结果与实验结果进行比较，并讨论它们在解释蛋白质折叠机制中的用途。
We present the initial findings of a theoretical study of hydrogen bond formation between two formamide molecules in water and in carbon tetrachloride. These systems were chosen as the simplest models for secondary structure formation in the polar environment near the protein surface and the apolar environment of the protein interior. We have employed thermodynamic simulation methods to obtain absolute binding free energies and free energy profiles for the formation of peptide hydrogen bonds in the two solvents. We find that the amide hydroden bond is stable by 8·4 kcal/mol in CCl4, and by 0·3 kcal/mol in water. Our results indicate also that the hydrogen-bonded dimer is 2·2 kcal/mol more stable in water than it is in CCl4. We compare our results with those from experiment, and discuss their use in interpreting mechanisms of protein folding.