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Energetics of hydrogen bonds in peptides

机译：肽中氢键的能量学

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Hydrogen bonds and their relative strengths in proteins are of importance for understanding protein structure and protein motions. The correct strength of such hydrogen bonds is experimentally known to vary greatly from ≈ 5-6 kcal/mol for the isolated bond to ≈ 0.5-1.5 kcal/mol for proteins in solution. To estimate these bond strengths, here we suggest a direct novel kinetic procedure. This analyzes the timing of the trajectories of a properly averaged dynamic ensemble. Here we study the observed rupture of these hydrogen bonds in a molecular dynamics calculation as an alternative to using thermodynamics. This calculation is performed for the isolated system and contrasted with results for water. We find that the activation energy for the rupture of the hydrogen bond in a β-sheet under isolated conditions is 4.76 kcal/mol, and the activation energy is 1.58 kcal/mol for the same β-sheet in water, These results are in excellent agreement with observations and suggest that such a direct calculation can be useful for the prediction of hydrogen bond strengths in various environments of interest.
机译：氢键及其在蛋白质中的相对强度对于理解蛋白质结构和蛋白质运动非常重要。从实验上已知，这种氢键的正确强度相差很大，从孤立键的≈5-6 kcal / mol到溶液中蛋白质的≈0.5-1.5 kcal / mol。为了估计这些键的强度，我们在这里建议一种直接新颖的动力学程序。这分析了适当平均的动态合奏轨迹的时序。在这里，我们研究分子动力学计算中观察到的这些氢键的断裂，以替代使用热力学。此计算是针对隔离的系统执行的，并与水的结果进行对比。我们发现，在分离条件下，β-折叠中氢键断裂的活化能为4.76 kcal / mol，相同的β-折叠在水中的活化能为1.58 kcal / mol，这些结果非常好。与观察结果一致，并表明这种直接计算可用于预测各种感兴趣的环境中的氢键强度。

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