Isothermal titration calorimetry (ITC) is a laboratory technique used to measure the heat released or absorbed when molecules interact, providing a direct, label-free way to characterize binding. As one substance is titrated into a solution containing its binding partner at constant temperature, the instrument recor…
Isothermal titration calorimetry (ITC) is a laboratory technique used to measure the heat released or absorbed when molecules interact, providing a direct, label-free way to characterize binding. As one substance is titrated into a solution containing its binding partner at constant temperature, the instrument records the tiny changes in heat that accompany each binding event. From these measurements, researchers can determine the strength of an interaction, the number of binding sites, and a complete thermodynamic profile, including binding affinity, enthalpy, and entropy. Because it works in solution without requiring labels or immobilization, ITC is widely applied to study protein-ligand binding, protein-protein and protein-nucleic acid interactions, enzyme kinetics, and the stability of molecular complexes. The thermodynamic detail it provides is valuable in biochemistry, structural biology, and drug discovery, where understanding how tightly and why molecules bind guides the design of new compounds. As a topic within Biotechnology and Biomedical Science, ITC connects biophysical measurement with molecular research. This page gathers peer-reviewed, open-access research relevant to molecular interactions and biophysical characterization, supporting researchers and students who study how biomolecules bind and assemble.
1 peer-reviewed article, ranked by relevance. Each links to its DOI.