Using the thermodynamic data from ITC, it is possible to deduce enzyme kinetics including proton or electron transfer, allostery and cooperativity, and enzyme inhibition. ITC collects data over time that is useful for any kinetic experiments, but especially with the proteins due to constant aliquots of injections. In terms of calculation, equilibrium constant and the slopes of binding can be directly utilized to determine the allostery and charge transfer, by comparing experimental data of different conditions (pH, use of mutated peptide chain and binding sites, etc.) .