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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Calculation of the standard molal thermodynamic properties of aqueous biomolecules at elevated temperatures and pressures II. Unfolded proteins.
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Calculation of the standard molal thermodynamic properties of aqueous biomolecules at elevated temperatures and pressures II. Unfolded proteins.

机译：在升高的温度和压力下计算水性生物分子的标准摩尔热力学性质II。未折叠的蛋白质。

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摘要

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.
机译：完全展开的蛋白质的状态方程已通过基团加和算法和经修订的Helgeson-Kirkham-Flowers（HKF）状态方程生成，以计算这些分子在高温和高压下的标准摩尔热力学性质。根据通过文献报道的实验量热和密度数据的回归获得的各组方程，计算出状态参数的必要方程。对于任何已知氨基酸序列的完全未折叠的蛋白质，该方法都允许根据温度和压力计算标准摩尔热力学性质。已经对11种嗜热蛋白进行了这类计算。可以将下面报告的热力学性质与蛋白质解折叠的热力学性质结合起来，以计算出完全折叠（即天然）蛋白质的相应性质。

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