Journal of Biological Chemistry · 1967 · 173 citations · 17 references
Life SciencesBiochemistryBiophysicsProtein BiochemistryStructural BiochemistryStructural BiologyFolding ThermodynamicsProtein Folding ThermodynamicsProtein StructureSecondary StructureSecondary Structure FormationDenaturation TemperatureHeat-induced DenaturationHeat-induced Protein DenaturationOptical Rotation MeasurementProtein Thermal StabilityTemperature-dependent Structural ChangesThermal Denaturation StudiesThermal Transitions
Abstract Ribonuclease, lysozyme, and chymotrypsinogen undergo thermal transitions at low pH, which have been studied in considerable detail in several laboratories. This paper shows, by measurement of optical rotation, that the products of these transitions retain regions of ordered structure, susceptible to disruption by guanidine hydrochloride.
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