Sound data for confirmation and prioritization
In addition to the SPR, NMR and native-MS expertize, NovALiX routinely perform other important orthogonal techniques for the characterization of protein ligand association. These are principally isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC) in order to strengthen the data set relating to any set validated binders to a target.
Isothermal titration calorimetry
ITC tends to be used as a secondary or orthogonal technique providing real-time label-free direct measurements binding constant (kD), stoichiometry (n) of binding and thermodynamic parameters of interactions in solution. ITC is unique in being able to measure changes in the two thermodynamic parameters the enthalpy (ΔH) and entropy (ΔS) that define the binding affinity.
Differential scanning calorimetry
DSC is able to show shifts of protein melting temperature (Tm) that occurs upon ligand binding. DSC quickly establishes if ligand binding to a protein gives a stabilized complex. Unlike ITC, DSC may enable correlation of the thermodynamics that drive binding with conformational changes in the macromolecule caused by the binding reaction. DSC is particularly useful in characterizing very tight binding interactions.