a Institute of Cell Biophysics, Russian Academy of Sciences , Pushchino , Moscow Region 142290 , Russia.
b Institute of Theoretical and Experimental Biophysics , Russian Academy of Sciences , Pushchino , Moscow Region 142290 , Russia.
J Biomol Struct Dyn. 2018 Feb;36(3):701-710. doi: 10.1080/07391102.2017.1294112. Epub 2017 Mar 14.
The analysis of temperature-induced unfolding of proteins in aqueous solutions was performed. Based on the data of thermodynamic parameters of protein unfolding and using the method of semi-empirical calculations of hydration parameters at reference temperature 298 K, we obtained numerical values of enthalpy, free energy, and entropy which characterize the unfolding of proteins in the 'gas phase'. It was shown that specific values of the energy of weak intramolecular bonds (∆H), conformational free energy (∆G) and entropy (∆S) are the same for proteins with molecular weight 7-25 kDa. Using the energy value (∆H) and the proposed approach for estimation of the conformational entropy of native protein (S), numerical values of the absolute free energy (G) were obtained.
对蛋白质在水溶液中温度诱导变性的过程进行了分析。基于蛋白质变性的热力学参数数据，并使用在参考温度 298 K 下半经验计算水合参数的方法，我们得到了在“气相”中表征蛋白质变性的焓、自由能和熵的数值。结果表明，分子量为 7-25 kDa 的蛋白质的弱分子内键的能量（∆H）、构象自由能（∆G）和熵（∆S）的特定值是相同的。利用能量值（∆H）和所提出的用于估计天然蛋白质构象熵（S）的方法，得到了绝对自由能（G）的数值。
