[Proton magnetic relaxation and thermodynamic parameters of ribonuclease solutions during thermal denaturation]

Heat denaturation of ribonuclease in diluted water solutions was studied by means of proton magnetic relaxation, microcalorimetry and viscosity. It has been shown that heat denaturation of ribonuclease is a one stage process; it involves the whole globule and is accompanied by changes in the state of salvated (water) molecules. A redistribution of water molecules in the hydrate "envelope" of protein changes the character of proton magnetic relaxation of the whole solvent.