Temperature-induced phase transitions in proteins and lipids. Volume and heat capacity effects.

Abstract

The partial specific heat capacity and volume of globular proteins and dispersions of phosphatidylcholines in aqueous solutions have been determined over a broad temperature range using a precise scanning microcalorimeter and a vibrational densimeter. It is shown that the temperature-induced, gel-to-liquid crystalline phase transition in phosphatidylcholines proceeds without a noticeable change in heat capacity but with a significant increase in the specific volume, whereas heat denaturation in proteins takes place without a noticeable change in the volume but with a significant increase in heat capacity. This principal difference between temperature-induced conformational phase transitions in proteins and lipids demonstrates clearly that heat denaturation of proteins, in contrast to the gel-to-liquid crystalline phase transition in lipids, cannot be regarded as a process similar to melting. Consequently, the 'molten globule' does not appear to be a suitable model for a heat-denatured protein.