Classical nucleation theory from a dynamical approach to nucleation
Classical nucleation theory from a dynamical approach to nucleation
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DOI：
10.1063/1.4811490
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发表时间：
2013-06-28
影响因子：
4.4
通讯作者：
Duran-Olivencia, Miguel A.
中科院分区：
文献类型：
--
作者：
Lutsko, James F.;Duran-Olivencia, Miguel A.
结果表明，扩散限制的经典成核理论（CNT）可以恢复为最近提出的基于波动流体力学的成核动力学理论的一个简单的限制[J. F。Lutsko，J.Chem.Phys.136，034509（2012）]。同样的框架也被用来构建一个更现实的理论，其中集群有有限的界面宽度。当应用于球状蛋白质的稀溶液/浓溶液转变时，发现即使对于由于单体分布函数和过量自由能的变化而导致的小过饱和的情况，扩展也对成核速率进行了修正。它也被发现，单体的附着/脱离的图片打破了在高过饱和度对应的集群小于约100个分子。结果也证实了通常的假设，最重要的修正CNT可以实现通过改进的估计的自由能垒。该理论还说明了两个主题，已收到相当大的关注，在最近的文献成核的重要性次主导修正的毛细管模型的自由能和正确选择的反应坐标。(C)2013 AIP Publishing LLC.
It is shown that diffusion-limited classical nucleation theory (CNT) can be recovered as a simple limit of the recently proposed dynamical theory of nucleation based on fluctuating hydrodynamics [J. F. Lutsko, J. Chem. Phys. 136, 034509 (2012)]. The same framework is also used to construct a more realistic theory in which clusters have finite interfacial width. When applied to the dilute solution/dense solution transition in globular proteins, it is found that the extension gives corrections to the nucleation rate even for the case of small supersaturations due to changes in the monomer distribution function and to the excess free energy. It is also found that the monomer attachment/detachment picture breaks down at high supersaturations corresponding to clusters smaller than about 100 molecules. The results also confirm the usual assumption that most important corrections to CNT can be achieved by means of improved estimates of the free energy barrier. The theory also illustrates two topics that have received considerable attention in the recent literature on nucleation: the importance sub-dominant corrections to the capillary model for the free energy and of the correct choice of the reaction coordinate. (C) 2013 AIP Publishing LLC.