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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:离子对天然聚集蛋白的稳定性和展开过渡的离子特异性影响; 重新认可

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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COLI RECA蛋白是一种天然聚集的蛋白质复合物,其受到盐存在的影响。为了进一步了解在天然聚集的蛋白质上的离子相互作用的性质,我们使用圆形二色性(CD),荧光和动态光散射(DLS)来研究不同浓度MgCl_2,CaCl_2,NaCl,Na_2SO_4的影响和reca结构和热展开的Mgso_4。结果显示了对RECA结构,聚集,展开转变和稳定性的独特离子影响,并且阴离子效果与反向Hofmeister系列相关。离子诱导的变化的机制最有可能由特定的离子结合,界面张力的变化和改变的蛋白质 - 溶剂相互作用,这对于天然聚集蛋白中的蛋白质 - 蛋白质相互作用可能尤为重要。一些离子的存在导致形成耐腐蚀以完全变性和非特异性聚集的重量复合物。

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