COMMON FEATURES OF PROTEIN UNFOLDING AND DISSOLUTION OF HYDROPHOBIC COMPOUNDS
COMMON FEATURES OF PROTEIN UNFOLDING AND DISSOLUTION OF HYDROPHOBIC COMPOUNDS
复制标题
DOI：
10.1126/science.2300815
复制
发表时间：
1990-02-02
期刊：
影响因子：
56.9
通讯作者：
GILL, SJ
中科院分区：
文献类型：
--
作者：
MURPHY, KP;PRIVALOV, PL;GILL, SJ
蛋白质的展开和疏水化合物（包括固体、液体和气体）在水中的溶解具有熵变和热容变化之间的线性关系。不同种类的化合物都有相同的斜率，而截距则取决于特定的种类。这些工艺的共同特点是将疏水性基团暴露于水中。这些观察结果使得将热容变化分配给疏水溶剂化成为可能，并根据疏水和非疏水贡献来描述蛋白质的稳定性。蛋白质稳定性的一般表示是由热容变化和温度给出的。
Protein unfolding and the dissolution of hydrophobic compounds (including solids, liquids, and gases) in water are characterized by a linear relation between entropy change and heat capacity change. The same slope is found for various classes of compounds, whereas the intercept depends on the particular class. The feature common to these processes is exposure of hydrophobic groups to water. These observations make possible the assignment of the heat capacity change to hydrophobic solvation and lead to the description of protein stability in terms of a hydrophobic and a nonhydrophobic contribution. A general representation of protein stability is given by the heat capacity change nad the temperature.