The Isothermal Calorimeter (iTC) investigates the production or absorption of heat from molecular interactions, reaction kinetics, and thermodynamics between molecules or a chemical reaction.
The iTC is the only equipment that can directly measure the energetics of biochemical processes involving interaction between two molecules such as a receptor and a ligand. A receptor can be any biopolymer such as a protein/enzyme, nucleic acid, carbohydrate, lipid etc, whereas a ligand can be either a large or small molecule (such as a metal, drug, inhibitor, activator, toxin, substrate, protein/peptide, sugar etc).
In addition to determining the affinity and stoichiometry of molecular binding, iTC has the ability to precisely measure the free energy, enthalpy, entropy and heat-capacity changes associated with binding and reaction. The current iTC200 requires only 0.2 mL of sample and 0.04 mL of titrant, is highly sensitive (can detect a heat signal of 0.2 µcal/sec) and takes less than an hour. iTC200 can also be upgraded to provide sample throughput of up to 50 samples per day with a capacity to process 384 samples unattended.