Pfeil W, Privalov P L
Biophys Chem. 1976 Jan;4(1):23-32. doi: 10.1016/0301-4622(76)80003-8.
A direct method is proposed for obtaining thermodynamic standard functions for native and denatured proteins using experimental data from scanning calorimetry, isothermal calorimetry and potentiometric titrations. The possibility of this approach is demonstrated on the example of lysozyme in the range of pH 1.5-7.0 and temperature 0-100 degrees C. Tests for the validity of the obtained functions of enthalpy and entropy are presented in the form of cyclic processes using experimental data obtained from thermodynamically different pathways. The Gibbs function is checked by comparison with results of an independent method. The methodic problems in determining and checking standard functions for proteins are discussed in detail.
提出了一种直接方法,用于利用扫描量热法、等温量热法和电位滴定法的实验数据获得天然蛋白质和变性蛋白质的热力学标准函数。以溶菌酶为例,在pH值1.5 - 7.0和温度0 - 100℃范围内证明了该方法的可行性。利用从热力学不同途径获得的实验数据,以循环过程的形式给出了对所获得的焓和熵函数有效性的检验。通过与独立方法的结果进行比较来检验吉布斯函数。详细讨论了确定和检验蛋白质标准函数时的方法问题。