[Formation and melting of ordered structures in denatured myoglobin with differing water content: differential scanning calorimetry method].

The possibility of superstructure formation in denatured globular proteins has been studied through the temperature dependence of the absolute values of heat capacity in the myoglobin-water system with water content from 80 to 25% in the temperature range 20-160 degrees C. For all the composition range studied it is found that after the denaturation of myoglobin the new regular structures with reversible melting are formed. These structures are similar in properties to the thermotropic gels in concentrated myoglobin solutions. Decrease of the water content influences the formation of these non-native ordered structures in denatured protein and increases the dispersion of its formation and melting temperatures.