[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.
D006358:Hot Temperature; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011489:Protein Denaturation; D011522:Protons; D012260:Ribonucleases; D013816:Thermodynamics; D014783:Viscosity; D014867:Water
D011522:Protons; D014867:Water; D012260:Ribonucleases
Protonnaia magntinaia relaksatsiia i termodinamicheskie parametry rastvorov ribonukleazy pri teplovoĭ denaturatsii.