蛋白质在疏水色谱中的变性热力学

研究21-80℃温度范围内一些蛋白质和小分子在疏水相互作用色谱中的热行为。利用Van't Hoff作图(lnk'-1/T)测定蛋白质分子的热力学参数(ΔH°, ΔS°和ΔG°), 根据标准熵变(ΔS°)和标准自由能变(ΔG°)判断蛋白质在色谱过程中的构象变化, 通过ΔH°-ΔS°的线性关系估计蛋白质变性时的"补偿温度"(β), 鉴定蛋白质在疏水相互作用色谱中保留机理的同一性。

Denatured thermodynamics for proteins in hydrophobic interaction chromatography

The thermodynamic behaviors for some proteins and small molecules in hydrophobic interaction chromatography are studied in the temperature range of 21-80℃. The thermodynamic parameters (ΔH°, ΔS°, ΔG°) of these proteins are determined by using Van't Hoff relationship (lnk'-1/T). By using the obtained standard entropy change (ΔS°) and free energy change (ΔG°), the conformational change of the proteins is judged in chromatographic process. The linear relationships between ΔH° and ΔS° can be used to evaluate "compensation temperature" (β) at the protein denaturation and identify the identity of the protein retention mechanism in hydrophobic interaction chromatography.