The molecular interactions that promote the stability of proteins and amino acids in saline solutions is a central topic of molecular biophysics. However, a well-supported molecular picture of the phenomena has not been established yet. In this paper, we studied as model system the mix between DL-Alanine in aqueous solutions of STP (Na₂S₂O₃5H₂O) at different temperatures, from volumetric and viscometric properties. The thermophysical properties obtained indicate the presence of a strong preferential solvation, structure-making action and a possible salt in effect. Quantum chemical calculations and molecular dynamic (MD) simulations provide a new insight to support these arguments.

中文翻译：

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DL-丙氨酸与电解环境分子相互作用的理论和实验方法。

促进盐溶液中蛋白质和氨基酸稳定性的分子相互作用是分子生物物理学的中心课题。但是，尚未建立对该现象的良好分子支持。在本文中，我们从体积和粘度特性的角度研究了不同温度下STP（Na ₂ S ₂ O ₃ 5H ₂ O）水溶液中DL-丙氨酸的混合物作为模型系统。获得的热物理性质表明存在强烈的优先溶剂化，结构形成作用和可能存在的盐。量子化学计算和分子动力学（MD）模拟为支持这些论点提供了新的见解。