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Updated: Jun 20, 2026
Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
Published on: September 13, 2014
Direct allowance for the effects of thermodynamic nonideality in the quantitative characterization of protein
Peter R Wills1, Donald J Winzor
1School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland 4072, Australia.
Abstract:
A procedure is described for the direct analysis of osmotic pressure data for reversibly dimerizing proteins that makes allowance for effects of thermodynamic nonideality on the statistical-mechanical basis of the potential-of-mean-force between molecules. Detailed consideration is also given to calculation of the magnitudes of the required virial coefficients. After illustration of the approach with analysis of simulated osmotic pressure data, the method is used to obtain dimerization constants from published osmotic pressure data for soybean proteinase inhibitor, hemoglobin and alpha-chymotrypsin.
