During the past decade, isothermal titration calorimetry (ITC) has developed from a specialist method to a major, commercially available tool in the arsenal directed at understanding molecular interactions. At present, ITC is used to study all types of binding reactions, including protein-protein, protein-ligand, DNA-drug, DNA-protein, receptor-target, and enzyme kinetics, and it is becoming the method of choice for the determination of the thermodynamic parameters associated with the structure transformation of one molecule or non-covalent interaction of two (or more) molecules. Here, the new applications of ITC in protein folding/unfolding and misfolding, as well as its traditional application in molecular interaction/recognition are reviewed, providing an overview of what can be achieved in these fields using this method and what developments are likely to occur in the near future.

Isothermal titration calorimetry, Protein folding/unfolding and misfolding, Molecular interaction/recognition

Keywords:

(Received 3 May 2006, Accepted 18 June 2006)