Amend J P, Helgeson H C
Department of Earth and Planetary Sciences, Washington University, St. Louis, MO 63130, USA.
Biophys Chem. 2000 Apr 14;84(2):105-36. doi: 10.1016/s0301-4622(00)00116-2.
Equations of state for completely unfolded proteins have been generated from group additivity algorithms and the revised Helgeson-Kirkham-Flowers (HKF) equations of state to compute the standard molal thermodynamic properties of these molecules at elevated temperatures and pressures. The requisite equations of state parameters were computed from those of groups retrieved by regression of experimental calorimetric and densimetric data reported in the literature. This approach permits calculation of the standard molal thermodynamic properties as a function of temperature and pressure for any completely unfolded protein for which the amino acid sequence is known. Calculations of this kind have been carried out for 11 thermophilic proteins. The thermodynamic properties reported below can be combined with those for protein unfolding to compute the corresponding properties of completely folded (i.e. native) proteins.
完全展开蛋白质的状态方程已通过基团加和算法以及修正的Helgeson-Kirkham-Flowers（HKF）状态方程生成，以计算这些分子在高温高压下的标准摩尔热力学性质。所需的状态方程参数是根据文献中报道的实验量热和密度数据回归得到的基团参数计算得出的。这种方法允许计算任何已知氨基酸序列的完全展开蛋白质的标准摩尔热力学性质随温度和压力的变化。已对11种嗜热蛋白质进行了此类计算。下面报道的热力学性质可与蛋白质折叠的性质相结合，以计算完全折叠（即天然）蛋白质的相应性质。
