Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water.
Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water.
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DOI：
10.1021/bi00131a009
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发表时间：
1992-04
期刊：
影响因子：
2.9
通讯作者：
Ruth S. Spolar;Jeff R. Livingstone;M. Record
中科院分区：
文献类型：
--
作者：
Ruth S. Spolar;Jeff R. Livingstone;M. Record
这种扩展的液态烃模型的目的是量化的热力学贡献蛋白质的稳定性从去除非极性和极性表面从水中。烃和有机酰胺从水转移到纯液相的热力学数据进行了分析，以获得从水可及表面积的减少折叠的热力学的贡献。虽然去除非极性表面的标准热容量变化的折叠（Δ C 0倍）的主要贡献，在这里，我们表明，包括从去除极性表面的贡献允许定量预测Δ C 0倍内的热量测定值的不确定性。此外，极性表面积的液体酰胺的转移焓的贡献的分析提供了一种手段，估计从非极性和极性表面积的变化，以及其他因素的折叠焓（Δ H 0倍）的贡献。除了Δ H 0倍的估计之外，液态烃模型的这种扩展为观察提供了热力学解释[Privalov，P.L.，& Khechinashvili，N. N.等（1974）J. Mol. Biol.86，665-684]，许多球状蛋白质的折叠比焓（cal g-1）在约383 K下收敛到一个共同值。由于折叠时被这些蛋白质掩埋的非极性和极性表面积的量被发现是摩尔质量的线性函数，因此仅给定感兴趣的蛋白质的摩尔质量就可以获得Δ C 0倍和Δ H 0倍的估计值。（250字处删节）
This extension of the liquid hydrocarbon model seeks to quantify the thermodynamic contributions to protein stability from the removal of nonpolar and polar surface from water. Thermodynamic data for the transfer of hydrocarbons and organic amides from water to the pure liquid phase are analyzed to obtain contributions to the thermodynamics of folding from the reduction in water-accessible surface area. Although the removal of nonpolar surface makes the dominant contribution to the standard heat capacity change of folding (delta C0fold), here we show that inclusion of the contribution from removal of polar surface allows a quantitative prediction of delta C0fold within the uncertainty of the calorimetrically determined value. Moreover, analysis of the contribution of polar surface area to the enthalpy of transfer of liquid amides provides a means of estimating the contributions from changes in nonpolar and polar surface area as well as other factors to the enthalpy of folding (delta H0fold). In addition to estimates of delta H0fold, this extension of the liquid hydrocarbon model provides a thermodynamic explanation for the observation [Privalov, P. L., & Khechinashvili, N. N. (1974) J. Mol. Biol. 86, 665-684] that the specific enthalpy of folding (cal g-1) of a number of globular proteins converges to a common value at approximately 383 K. Because amounts of nonpolar and polar surface area buried by these proteins upon folding are found to be linear functions of molar mass, estimates of both delta C0fold and delta H0fold may be obtained given only the molar mass of the protein of interest.(ABSTRACT TRUNCATED AT 250 WORDS)