Bonner O D
Physiol Chem Phys. 1978;10(1):25-35.
Isopiestic equilibration measurements were made on ten protein-denaturant systems involving polyglycine, egg albumin, collagen, horse heart myoglobin, and the denaturants urea, 1,3-dimethylurea, 1,1-dimethylurea, and thiourea. The hydration of the proteins in the absence of denaturants is a function of the water activity and it is believed that this accounts, at least in part, for the varying hydration values found in the literature. The relative binding of water and denaturant to unfolded proteins was found to be a reversible process for which an equilibrium constant can be calculated. It was further found that in most cases the protein binds denaturant preferentially to water even in aqueous systems.
对十个蛋白质-变性剂体系进行了等压平衡测量，这些体系涉及聚甘氨酸、蛋清蛋白、胶原蛋白、马心肌红蛋白以及变性剂尿素、1,3-二甲基脲、1,1-二甲基脲和硫脲。在没有变性剂的情况下，蛋白质的水合作用是水活度的函数，据信这至少部分解释了文献中发现的不同水合值。发现水和变性剂与未折叠蛋白质的相对结合是一个可逆过程，为此可以计算平衡常数。还进一步发现，在大多数情况下，即使在水性体系中，蛋白质也优先结合变性剂而非水。
