Determination of Accurate Thermodynamics of Binding for Proteinase-Inhibitor Interactions
The affinity of a low-molecular weight ligand to a macromolecular target protein is usually described by the binding constant Ki that typically corresponds to a negative free energy of binding of 10–80 kJ/mol in aqueous solution. It comprises enthalpic and entropie contributions that arise from several underlying phenomena. To better understand and subsequently describe the binding process detailed measurements of these quantities are required.
KeywordsEthyl Enthalpy Titration Trypsin Calorimetry