On the physics of pressure denaturation of proteins
On the physics of pressure denaturation of proteins
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DOI：
10.1088/0953-8984/18/7/l01
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发表时间：
2006-02-22
影响因子：
2.7
通讯作者：
Kinoshita, M
中科院分区：
文献类型：
--
作者：
Harano, Y;Kinoshita, M
我们发现，水分子的平移运动引起的熵效应在压力诱导的蛋白质变性中起着关键作用。在我们的统计力学方法中，控制结构稳定性的压力依赖性的偏摩尔体积表示为每个蛋白质结构的两个几何测量，水分子的排除体积和可达表面积，以及与表面附近熵形成的水密度剖面相关的参数。一个未展开的结构在高压下比天然结构更稳定，成功地表现了实验观察到的变性。
We show that the entropic effect originating from the translational movement of water molecules plays critical roles in the pressure-induced denaturation of proteins. In our statistical-mechanical method, the partial molar volume governing the pressure dependence of the structural stability is expressed in terms of the two geometric measures of each protein structure, the excluded volume and the accessible surface area for water molecules, and a parameter related to the water-density profile entropically formed near its surface. An unfolded structure, which is shown to turn more stable than the native one at an elevated pressure, successfully features the experimentally observed denaturation.