Thermodynamic Properties of Supersaturated Protein Solutions
Thermodynamic Properties of Supersaturated Protein Solutions
复制标题
过饱和蛋白质溶液的热力学性质
DOI：
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发表时间：
2004
期刊：
影响因子：
--
通讯作者：
A. Myerson
中科院分区：
文献类型：
--
作者：
Dragutin Knezic;J. Zaccaro;A. Myerson
本工作的目的是研究水和蛋白质（溶菌酶）在过饱和水溶液中的活动。电动悬浮阱（ELT）用于悬浮单个带电的蛋白质水溶液液滴，而无需容器。该技术允许调查均匀成核和测量水的活性深入到过饱和液滴的亚稳区。该体系被视为三元体系（蛋白质+溶剂+“理想”盐），蛋白质活性采用吉布斯-杜亨方程计算。对数（α蛋白/）随蛋白浓度的变化趋势最初显示急剧增加，但随后在更高的蛋白浓度下，趋势开始趋于平稳。在盐水系统和有机水系统中可以看到相同的趋势，并且遵循过饱和溶液的预期行为。随着体系越来越接近旋节曲线，溶液的吉布斯自由能相对于质子的二阶导数也随之增大。
The purpose of this work is to investigate water and protein (lysozyme) activities in supersaturated aqueous protein solutions. An electrodynamic levitation trap (ELT) is used to suspend a single charged droplet of aqueous protein solution without a container. This technique allows investigation of homogeneous nucleation and measurements of water activity deep into the metastable zone of a supersaturated droplet. The system was treated as a ternary one (protein + solvent + “ideal” salt), and the protein activity is calculated employing the Gibbs−Duhem equation. The trend of logarithm (aprotein/ ) with protein concentration shows initially a sharp increase, but then at higher protein concentrations the trend starts to level off. The same trend is seen in salt-water systems and organic−water systems and follows the expected behavior of supersaturated solutions. As the system is brought closer and closer to the spinodal curve, the second derivative of the Gibbs free energy of the solution with respect to pro...
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影响因子：
2.9
作者：
ARAKAWA, T;TIMASHEFF, SN
通讯作者：
TIMASHEFF, SN
影响因子：
2.9
作者：
ARAKAWA, T;TIMASHEFF, SN
通讯作者：
TIMASHEFF, SN
影响因子：
15
作者：
Yau, ST;Vekilov, PG
通讯作者：
Vekilov, PG
影响因子：
2.9
作者：
ARAKAWA, T;TIMASHEFF, SN
通讯作者：
TIMASHEFF, SN