چكيده لاتين :
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.
