[Ribonuclease hydration and its heat stability in solutions of H2O and D2O].
Ribonuclease hydration in wide concentration and temperature range using differential scanning microcalorimetry and NMR technique was studied. The temperature- concentration equilibrium diagram for H2O--ribonuclease system was suggested. Protein hydration in D2O was shown to be higher than in ordinary water. NMR measurements in dilute protein solutions showed that cooperative temperature denaturation was followed by solvation changes. Models of globular protein hydration are discussed.
D002152:Calorimetry, Differential Scanning; D055598:Chemical Phenomena; D002621:Chemistry; D002627:Chemistry, Physical; D003903:Deuterium; D006358:Hot Temperature; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D010179:Pancreas / Q000201:enzymology; D011487:Protein Conformation; D011489:Protein Denaturation; D011522:Protons; D012260:Ribonucleases; D012996:Solutions; D013816:Thermodynamics; D014867:Water
D011522:Protons; D012996:Solutions; D014867:Water; D003903:Deuterium; D012260:Ribonucleases
Gidratsiia ribonukleazy i ee termicheskaia stabil'nost' v rastvorakh H2O i D20.