[Denaturation increment of heat capacity in diluted aqueous solutions of collagen]

The experimental values of the denaturation increment of collagen heat capacity in diluted aqueous solutions, obtained at different scanning rates, are presented. It is shown that the dependences of the "equilibrium" enthalpy and entropy of collagen denaturation on denaturation-induced variation in heat capacity do not obey the empiric law of the linear correlation of the thermodynamic parameters of denaturation at 25 degrees C for globular proteins, indicating that the stabilization of the triple collagen helix proceeds by a special mechanism with the participation of water molecules.