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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Ion specific influences on the stability and unfolding transitions of a naturally aggregating protein; RecA
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Ion specific influences on the stability and unfolding transitions of a naturally aggregating protein; RecA

机译:离子特异性影响天然聚集蛋白的稳定性和展开过渡;收录机

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摘要

The Escherichia coli RecA protein is a naturally aggregated protein complex that is affected by the presence of salts. In order to gain further insight into the nature of the ion-interactions on a naturally aggregating protein we used circular dichroism (CD), fluorescence and dynamic light scattering (DLS) to study the effects of different concentrations of MgCl_2, CaCl_2, NaCl, Na_2SO_4, and MgSO_4 on RecA structure and thermal unfolding. The results show unique ion influences on RecA structure, aggregation, unfolding transitions and stability and the anion effects correlate with the reverse Hofmeister series. The mechanisms of the ion-induced changes most likely result from specific ion binding, changes in the interfacial tension and altered protein-solvent interactions that may be especially important for protein-protein interactions in naturally aggregating proteins. The presence of some ions leads to the formation of RecA complexes that are resistant to complete denaturation and nonspecific aggregation.
机译:大肠杆菌RecA蛋白是一种天然聚集的蛋白质复合物,受盐的存在影响。为了进一步了解天然聚集蛋白上离子相互作用的性质,我们使用圆二色性(CD),荧光和动态光散射(DLS)研究了不同浓度的MgCl_2,CaCl_2,NaCl,Na_2SO_4的影响,以及MgSO_4的RecA结构和热展开。结果表明,离子对RecA的结构,聚集,展开转变和稳定性具有独特的影响,并且阴离子效应与反向Hofmeister系列相关。离子诱导的变化的机制最有可能是由于特定的离子结合,界面张力的变化以及蛋白质-溶剂相互作用的改变,这对于天然聚集蛋白质中的蛋白质-蛋白质相互作用可能尤其重要。一些离子的存在导致形成对完全变性和非特异性聚集有抵抗力的RecA复合物。

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