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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >On the stabilizing action of protein denaturants: acetonitrile effect on stability of lysozyme in aqueous solutions.
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On the stabilizing action of protein denaturants: acetonitrile effect on stability of lysozyme in aqueous solutions.

机译：关于蛋白质变性剂的稳定作用：乙腈对水溶液中溶菌酶稳定性的影响。

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摘要

Stability of hen lysozyme in the presence of acetonitrile (MeCN) at different pH values of the medium was studied by scanning microcalorimetry with a special emphasis on determination of reliable values of the denaturational heat capacity change. It was found that the temperature of denaturation decreases on addition of MeCN. However, the free energy extrapolation showed that below room temperature the thermodynamic stability increases at low concentrations of MeCN in spite of the general destabilizing effect at higher concentrations and temperatures. Charge-induced contribution to this stabilization was shown to be negligible (no pH-dependence was found); therefore, the most probable cause for the phenomenon is an increase of hydrophobic interactions at low temperatures in aqueous solutions containing small amounts of the organic additive. The difference in preferential solvation of native and denatured states of lysozyme was calculated from the stabilization free energy data. It was found that the change in preferential solvation strongly depends on the temperature in the water-rich region. At the higher MeCN content this dependence decreases until, at 0.06 mole fractions of MeCN, the difference in the preferential solvation between native and denatured lysozyme becomes independent of the temperature over a range of 60 K. The importance of taking into account non-ideality of a mixed solution, when analyzing preferential solvation phenomena was emphasized.
机译：通过扫描微量量热法研究了在不同pH值条件下乙腈（MeCN）存在下的鸡溶菌酶的稳定性，并特别强调确定变性热容变化的可靠值。发现加入MeCN会使变性温度降低。然而，自由能推断显示，在室温以下，尽管在较高浓度和温度下具有一般的去稳定化作用，但在低浓度MeCN下，热力学稳定性仍会提高。电荷诱导的对该稳定作用的贡献可忽略不计（未发现pH依赖性）。因此，这种现象的最可能原因是在低温下，含有少量有机添加剂的水溶液中疏水相互作用增加。从稳定的自由能数据计算溶菌酶的天然和变性状态的优先溶剂化的差异。已经发现，优先溶剂化的变化很大程度上取决于富水区域中的温度。在较高的MeCN含量下，这种依赖性降低，直到在0.06摩尔分数的MeCN时，天然和变性溶菌酶之间优先溶剂化的差异变得独立于60 K范围内的温度。在分析优先溶剂化现象时强调混合溶液。

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