Differential scanning calorimetry as a tool to study protein-ligand interactions

Abstract

Differential scanning calorimetry can be used as an interesting tool to study protein-ligand interactions, with the aid of suitable thermodynamic models. This review analyzes and discusses results recently obtained in our laboratory with regard to the binding equilibrium of 2' and 3' cytidine monophosphate to RNAase A, the interaction of S-peptide with S-protein, the binding of D-glucose to yeast hexokinase and the thermal stability of respective complexes. © 1995 IUPAC