蛋白质结晶过程中团簇的奥斯特瓦尔德熟化。
Ostwald ripening of clusters during protein crystallization.
机构信息
Department of Applied Physics, Stanford University, Stanford, California 94305, USA.
出版信息
Phys Rev Lett. 2010 Apr 30;104(17):178102. doi: 10.1103/PhysRevLett.104.178102. Epub 2010 Apr 26.
Abstract
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.
摘要
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先于致密无定形相的成核。我们使用动态光散射、光学显微镜和微流控技术研究溶菌酶中这些预晶簇的生长。簇显示奥斯特瓦尔德成熟生长动力学，但在晶相成核后偏离此趋势。这种行为源于簇与有序固相之间的亚稳关系，并使用种群平衡模型进行数值解释。
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