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动力学因素可能会重塑蛋白质本体溶液中晶体成核速率对温度的依赖性。

Kinetic factors may reshape the dependence of crystal nucleation rate on temperature in protein bulk solution.

机构信息

Institute of Physical Chemistry "Rostislaw Kaischew", Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 11, 1113, Sofia, Bulgaria.

出版信息

J Biol Phys. 2020 Dec;46(4):343-350. doi: 10.1007/s10867-020-09558-1. Epub 2020 Oct 16.

Abstract

Here we provide an analysis of primary results obtained from a study of apoferritin crystal nucleation in compositionally invariant bulk solution at constant supersaturation ratio of the protein. The temperature dependence of the stationary crystal nucleation rate in the protein bulk solution is obtained with the help of experimentally determined probability for detection of at least one crystal per solution volume until a given time. The stationary crystal nucleation rate demonstrates unusual behavior with temperature. We emphasize that this is caused by kinetic factors that are often disregarded in the frame of the classical nucleation theory but can certainly affect the nucleation kinetics.

摘要

在这里,我们提供了对在组成不变的本体溶液中在恒定的蛋白质过饱和度比下进行脱铁蛋白晶体成核的研究中获得的主要结果的分析。通过实验确定的在给定时间内每溶液体积检测到至少一个晶体的概率,获得了蛋白质本体溶液中固定晶体成核速率的温度依赖性。固定晶体成核速率表现出异常的温度依赖性。我们强调,这是由动力学因素引起的,这些因素在经典成核理论的框架中经常被忽视,但肯定会影响成核动力学。

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