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The inverse and direct Hofmeister series for lysozyme

机译:Hofmeister溶菌酶的反向和直接系列

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摘要

Anion effects on the cloud-point temperature for the liquid-liquid phase transition of lysozyme were investigated by temperature gradient microfluidics under a dark field microscope. It was found that protein aggregation in salt solutions followed 2 distinct Hofmeister series depending on salt concentration. Namely, under low salt conditions the association of anions with the positively charged lysozyme surface dominated the process and the phase transition temperature followed an inverse Hofmeister series. This inverse series could be directly correlated to the size and hydration thermodynamics of the anions. At higher salt concentrations, the liquid-liquid phase transition displayed a direct Hofmeister series that correlated with the polarizability of the anions. A simple model was derived to take both charge screening and surface tension effects into account at the protein/water interface. Fitting the thermodynamic data to this model equation demonstrated its validity in both the high and low salt regimes. These results suggest that in general positively charged macromolecular systems should show inverse Hofmeister behavior only at relatively low salt concentrations, but revert to a direct Hofmeister series as the salt concentration is increased.
机译:在暗视野显微镜下,通过温度梯度微流控技术研究了溶菌酶液-液相转变过程中阴离子对浊点温度的影响。发现盐溶液中的蛋白质聚集遵循两个不同的Hofmeister系列,具体取决于盐浓度。即,在低盐条件下,阴离子与带正电荷的溶菌酶表面的结合占主导地位,并且相变温度遵循霍夫迈斯特逆系列。该反系列可以直接与阴离子的大小和水合热力学相关。在较高的盐浓度下,液-液相转变表现出直接的Hofmeister级数,该级数与阴离子的极化率相关。推导了一个简单的模型,该模型考虑了蛋白质/水界面处的电荷筛选和表面张力效应。将热力学数据拟合到该模型方程式,证明了其在高盐和低盐条件下的有效性。这些结果表明,通常带正电的大分子系统仅在相对较低的盐浓度下才应表现出逆Hofmeister行为,但随着盐浓度的增加,应恢复为直接的Hofmeister级数。

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