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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Thermodynamic study of protein phases formation and clustering in model water-protein-salt solutions.
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Thermodynamic study of protein phases formation and clustering in model water-protein-salt solutions.

机译：模型水-蛋白质-盐溶液中蛋白质相形成和聚集的热力学研究。

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摘要

Thermodynamic analysis of the water-protein-salt system, based on the description of the spinodal curve, has been carried out in various coordinate systems: (water chemical potential, protein concentration m(2)); (protein "solubility" log S, salt concentration m(3)); (effective temperature, critical composition of the system m(2)/m(3)). Such presentations explain the existence of diagrams with normal and retrograde protein solubility as a result of straightforward effect of ions present in solution as well as some features of the widely used phase diagram in coordinates (temperature, protein concentration). Analytic expressions for coefficients K and b of the salting out equation log S=-K.m(3)+b as functions of protein charge and protein adsorbed ions have been obtained and identified with the spinodal characteristic points reflecting quasi-equilibrium between protein-lean phase and dense protein-rich phase. Liquid-liquid, liquid-solid phase transitions, dynamic protein clusters and second virial coefficient that characterize interaction between solution components have been thus interrelated. The results of our thermodynamic analysis have been compared with the data reported for lysozyme .
机译：基于旋节线曲线的描述，水-蛋白质-盐系统的热力学分析已在各种坐标系中进行：（水化学势，蛋白质浓度m（2））; （蛋白质“溶解度” log S，盐浓度m（3））; （有效温度，系统的关键组成m（2）/ m（3））。这样的介绍解释了存在于溶液中的离子具有直接作用的结果以及正常和逆行蛋白质溶解度的图的存在，以及坐标（温度，蛋白质浓度）中广泛使用的相图的某些特征。获得了盐析方程log S = -Km（3）+ b作为蛋白质电荷和蛋白质吸附离子的函数的解析表达式，并确定了旋节线特征点，反映了稀蛋白质相之间的准平衡和致密的富含蛋白质的相。因此，表征了溶液组分之间相互作用的液-液，液-固相变，动态蛋白质簇和第二病毒系数已经相互关联。我们的热力学分析结果已与溶菌酶报告的数据进行了比较。

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