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

Mrevlishvili, G.M.; Sharimanov, I.G.

Biofizika 25(2): 338-340

1980


ISSN/ISBN: 0006-3029
PMID: 6245733
Document Number: 166708
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.

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