ArticleMethods in molecular biology (Clifton, N.J.)2026
Isothermal Titration Calorimetry for Investigating Thermodynamics of Protein-Lipid Interactions.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Isothermal titration calorimetry (ITC) is a remarkably versatile and powerful technique for studying the interactions between molecules. In ITC, intermolecular interactions are investigated by measuring heat changes (heat released/absorbed) occurring during the binding process. A very important feature of ITC is that it is a label-free technique and does not need any probe to be incorporated into the system. In view of this, it has become the method of choice for investigating the interaction of proteins with a wide range of species, including small ligands, other proteins, nucleic acids, drugs, nanoparticles, and metal ions. In recent years, ITC has gained popularity for studying protein interactions with lipids and lipid membranes as well. In this chapter, we provide a comprehensive overview of the ITC instrument and its practical application to determining the thermodynamic parameters characterizing the interaction between proteins and lipids. Employing ITC one can determine a variety of thermodynamic parameters, including enthalpy of binding (ΔH), binding stoichiometry (n), association constant (K
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