title: Isothermal titration calorimetry for studying protein-ligand interactions.
abstract: Isothermal titration calorimetry (ITC) is a biophysical technique that allows a thermodynamic characterization of an interactive system. It is a free in solution technique that requires no labeling, using heat as signal. ITC allows simultaneous determination of affinity K a, stoichiometry n, enthalpy change ΔH and calculation of free energy change ΔG and entropy change ΔS in one single experiment. It is the only technique that allows direct enthalpy change measurement. By accessing the enthalpy change, we get a step closer in estimating the driving forces that characterize the interaction of a protein with a ligand, information much needed in the drug discovery process.
authors.affiliation: Microcal Products, GE Healthcare, Little Chalfont, UK.
authors.forename: Luminita
authors.initials: L
authors.lastname: Damian
mesh_terms: D001667:Binding, Competitive; D002151:Calorimetry / Q000379:methods*; D055808:Drug Discovery; D006801:Humans; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008024:Ligands; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D013237:Stereoisomerism; D013816:Thermodynamics
chemical_list: D008024:Ligands; D011506:Proteins