Abstract
IN the field of thermodynamics of protein solutions, there are two kinds of denaturation induced by temperature changes. One of them is the commonest heat denaturation induced by temperature increasing and accompanied by a heat absorption and an increase of enthalpy and entropy. The other is cold denaturation, predicted by ~randts"] over thirty years ago: the compact ordered structure of protein molecules in the native state is induced into a disordered structure with temperature decreasing. The progress of cold denaturation is accompanied by a heat release and a decrease of enthalpy and entropy. The transformation from an ordered
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