Abstract
The effect of monohydric alcohols on the micellization of sodium dodecyl sulphate (SDS) and on the thermal unfolding of lysozyme has been studied by DSC as a function of alcohol concentration in the water-rich region of composition. The results show that the effects due to alcohols on these very different systems and processes are strikingly similar and are closely linked with structural and dynamical properties of water–alcohol mixtures themselves. The data have been interpreted on the basis of the assumption that the addition of short chain alcohol affects both the thermal unfolding of proteins as the micellization process modifying the extent of enthalpy and entropy contribution associated with structural reorganization of water in these processes.
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