Dias Cristiano L, Ala-Nissila Tapio, Karttunen Mikko, Vattulainen Ilpo, Grant Martin
Physics Department, Rutherford Building, McGill University, 3600 rue University, Montréal, Québec, Canada H3A 2T8.
Phys Rev Lett. 2008 Mar 21;100(11):118101. doi: 10.1103/PhysRevLett.100.118101. Epub 2008 Mar 18.
We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect induces, facilitates, and is the driving force for cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in favor of solvent-separated configurations, the same mechanism seen in pressure-induced denaturation. A phenomenological explanation proposed for the mechanism is suggested as being responsible for cold denaturation in real proteins.
我们通过对一种在显式溶剂中的疏水分子模型进行恒压模拟，阐明了冷变性的机制。我们发现疏水效应的温度依赖性诱导、促进了冷变性，并且是冷变性的驱动力。这种现象背后的物理机制被确定为疏水接触的不稳定，有利于溶剂分离的构型，这与压力诱导变性中观察到的机制相同。针对该机制提出的一种现象学解释被认为是真实蛋白质中冷变性的原因。
