International journal of peptide & protein research · 1976 · 14 citations · 25 references
Natural SciencesBiochemistryBiophysicsPhysical ChemistryProtein BiochemistryThermodynamicsEnzyme KineticsProtein StabilizationRibonucleic Acid (Rna) ChemistryRna BiophysicsTemperature ResponsesAdditive EffectsHeat-induced DenaturationHydrophobic SolvationRibonuclease ChemistryTemperature Effects On Enzyme ActivityThermal Denaturation Studies
The effects of a combination of an alcohol and urea on the transition temperature of bovine ribonuclease were investigated. The combined effects on the transition temperature of ribonuclease of a polyvalent alcohol and urea are about equal to the algebraic sum of the effects of each individual additive. The effects of a monovalent alcohol and urea are not cummulative, especially not at low temperatures (30 degrees C). The presence of urea decreases the hydrophobic effect of a monovalent alcohol, strongly at low temperatures, to a lesser degree at high temperatures (60 degrees C). Consequently, urea hinders the interhydrophobic interactions by affecting the water molecules.
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Principles that Govern the Folding of Protein Chains
Christian B. Anfinsen · Science · 1973 · 7.1K citations