Wintrode P L, Makhatadze G I, Privalov P L
Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218.
Proteins. 1994 Mar;18(3):246-53. doi: 10.1002/prot.340180305.
The energetics of ubiquitin unfolding have been studied using differential scanning microcalorimetry. For the first time it has been shown directly that the enthalpy of protein unfolding is a nonlinear function of temperature. Thermodynamic parameters of ubiquitin unfolding were correlated with the structure of the protein. The enthalpy of hydrogen bonding in ubiquitin was calculated and compared to that obtained for other proteins. It appears that the energy of hydrogen bonding correlates with the average length of the hydrogen bond in a given protein structure.
已使用差示扫描量热法研究了泛素展开的能量学。首次直接表明蛋白质展开的焓是温度的非线性函数。泛素展开的热力学参数与蛋白质的结构相关。计算了泛素中氢键的焓，并与其他蛋白质的进行了比较。结果表明，氢键能量与给定蛋白质结构中氢键的平均长度相关。
