Ostwald ripening of clusters during protein crystallization.
Ostwald ripening of clusters during protein crystallization.
复制标题
蛋白质结晶过程中簇成熟的成熟。
DOI：
10.1103/physrevlett.104.178102
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发表时间：
2010-04-30
影响因子：
8.6
通讯作者：
Quake SR
中科院分区：
文献类型：
--
作者：
Streets AM;Quake SR
与经典成核理论相反，蛋白质晶体可以通过两步过程成核，其中有序固相的分子排列之前是致密无定形相的成核。我们使用动态光散射、光学显微镜和微流体技术相结合的方法研究了这些晶体簇在溶菌酶中的生长。团簇显示奥斯特瓦尔德熟化生长动力学，但偏离这种趋势后，结晶相的成核。这种行为产生于簇和有序固体之间的亚稳关系，并使用种群平衡模型进行了数值解释。
Contrary to classical nucleation theory, protein crystals can nucleate via a two-step process in which the molecular arrangement of the ordered solid phase is preceded by nucleation of a dense amorphous phase. We study the growth of these precrystalline clusters in lysozyme using a combination of dynamic light scattering, optical microscopy, and microfluidics. Clusters display Ostwald ripening growth kinetics but deviate from this trend after nucleation of the crystal phase. This behavior arises from the metastable relationship between clusters and the ordered solid and is explained numerically using a population balance model.