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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >The affect of urea on the kinetics of local unfolding processes in chymotrypsin inhibitor 2.
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The affect of urea on the kinetics of local unfolding processes in chymotrypsin inhibitor 2.

机译：尿素对胰凝乳蛋白酶抑制剂2局部展开过程动力学的影响

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摘要

The dynamics of chymotrypsin inhibitor 2 (CI2) in water, as well as in 10M urea, have been studied by Molecular Dynamics simulations. The analysis aims at investigating how local protein processes are affected by urea and how the perturbation by urea on the local level manifests itself in the kinetics of the global unfolding. The results show that the effect of urea on local processes depends upon the type of process at hand. An isolated two-residue contact on the surface of CI2 has a decreased frequency of rupture in the urea solvent. This is in contrast to the increased frequency of rupture of the hydrogen bonds in secondary structure elements in the urea solvent. It is proposed that the increase in the unfolding rates of complex protein processes is based upon the retardation of the refolding rate of small scale, isolated processes.
机译：通过分子动力学模拟研究了胰凝乳蛋白酶抑制剂2（CI2）在水中以及在10M尿素中的动力学。该分析旨在研究尿素对局部蛋白质过程的影响，以及尿素在局部水平上的扰动如何在整体展开的动力学中体现出来。结果表明，尿素对局部过程的影响取决于当前过程的类型。在CI2表面上的孤立的两个残基接触减少了在尿素溶剂中的破裂频率。这与尿素溶剂中二级结构元素中氢键的断裂频率增加相反。提出复杂蛋白质过程的解折叠速率的增加是基于小规模分离过程的重折叠速率的延迟。

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