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Liquid-solid transition in nuclei of protein crystals.

机译:蛋白晶体核中的液固转变。

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摘要

It is generally assumed that crystallization begins with a small, crystalline nucleus. For proteins this paradigm may not be valid. Our numerical simulations show that under conditions typically used to produce protein crystals, small clusters of model proteins (particles with short-range, attractive interactions) cannot maintain a crystalline structure. Protein crystal nucleation is therefore an indirect, two-step process. A nucleus first forms and grows as a disordered, liquid-like aggregate. Once the aggregate grows beyond a critical size (about a few hundred particles) crystal nucleation becomes possible.
机译:通常认为结晶始于小的结晶核。对于蛋白质,此范例可能无效。我们的数值模拟表明,在通常用于生产蛋白质晶体的条件下,模型蛋白质的小簇(具有短距离,有吸引力的相互作用的粒子)不能保持晶体结构。因此,蛋白质晶体成核是一个间接的两步过程。核首先形成并生长为无序的液体状聚集体。一旦聚集体生长超过临界尺寸(约几百个颗粒),晶体成核就成为可能。

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