PEAQ-ITC microcalorimeter

Interactions between biomolecules play a crucial role in various cellular processes. These interactions can involve protein-protein, DNA-protein, lipid-protein, or protein-low molecular weight ligand interactions. To understand the functioning of proteins, nucleic acids, lipids, and other molecules in a biological system, it is essential to identify their interaction partners and characterize their interactions. The characterization of biomolecular interactions requires knowledge of affinity, the number of binding sites, and thermodynamic properties. By performing a simple ITC experiment, it is possible to determine parameters such as binding affinity (KD), stoichiometry, enthalpy (ΔH), and entropy (ΔS). Thermodynamic parameters such as ΔH and ΔS provide valuable insights into complex formation and possible conformational changes of a binding partner after the binding event. The Bioanalytic Core Facility offers the usage of the PEAQ-ITC microcalorimeter from Malvern. For more details about our PEAQ-ITC instrument, please visit the MalvernPanalytical