Abstract
Abstract The conformational changes of ribonuclease A due to thermal and guanidine hydrochloride denaturation were monitored by means of precise density and sound velocity measurements. The adiabatic compressibility and apparent partial molar volume decreased on guanidine hydrochloride denaturation, but thermal denaturation showed the increase in compressibility and the decrease in molar volume, as found for pressure denaturation. The compressibility change was not correlated to a loss of the secondary structure in the transition region. These results suggest that the conformation of protein partially denatured by guanidine hydrochloride, as well as by heat and pressure, remains as some molten-globule-like intermediates having the loose compactness and high flexibility.
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