Isothermal titration calorimetry (ITC) is one of the physical techniques used to directly measure the reaction process between biomolecules. It is an analytical method for determining the contact between ligands and macromolecules at a constant temperature. ITC uses the thermodynamic principle that the combination of two molecules will cause the generation or absorption of heat to determine the binding affinity, stoichiometry, entropy, and enthalpy of the binding reaction in the solution. The entire reaction can be carried out in the solution without the use of any labels, and without protein immobilization and chemical modification. Also, ITC technology will not be limited by the size of the protein or ligand, and the potential optical properties of the sample will not interfere with the experiment. Due to its excellent performance, ITC has been widely used to study the binding of inhibitors, substrates, peptides, and cofactors to a protein, and can provide quantitative results within a few hours. However, ITC requires a relatively high concentration of macromolecular samples.
Figure 1. Basic principle of isothermal titration calorimetry (Song, C.C.; et al. 2015)
Creative Proteomics introduced Microcal PEAQ-ITC (Malvern Panalytical) and other related equipment as well as experienced technical personnel, aiming to provide researchers around the world with first-class services in the fields of intermolecular interaction, self-association, and structural biology, etc.
Customers can choose different technology platforms according to project requirements, or contact us directly for consultation, and our expert team will provide you with customized experimental procedures.