Calorimetric Study of the Glass Transition Process in Humid Proteins and DNA

By method of differential scanning calorimetry the absolute values of heat capacity for the systemwater–biopolymer (globular and fibrillar proteins and DNA) were measured in a wide range of temperatures (from -30 up to 130°C) and concentrations of proteins both in native and denatured states. Thermal properties of humid denatured biopolymers demonstrate a characteristic anomaly in the form of the heat capacity jump at temperature depending on the bound water content. It has been shown that in the systems studied a glass transition, where water serves as a native plasticizer, is observed. It has been established that the S-shaped character of all heat capacity curves obtained on dehydration for native and denatured biopolymers is due to the gradual transition to the glassy state of both native and denatured samples. It was found that thermally denatured humid small globular proteins at subsequent dissolving in water at room temperature are able to restore their native structure. This revised version was published online in July 2006 with corrections to the Cover Date.