Abstract
Effects of β-cyclodextrin, βCD, on refolding of lysozyme was investigated at pH 12 employing isothermal titration calorimetry (ITC) at 300K in 30mM Tris buffer solution. βCD was employed as an anti-aggregation agent and the heats obtained for lysozyme+βCD interactions are reported and analyzed in terms of the extended solvation model. It was indicated that there are two sets of identical and non-cooperative sites for βCD.
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