Services
- Thermodynamic analysis of protein-protein and protein-ligand interaction through determination by isothermal titration microcalorimetry (ITC) of binding constants (KB), reaction stoichiometry (n), enthalpy (ΔH) and entropy (ΔS).
- Thermodynamic analysis of conformational changes of proteins including assessment of stability and folding of recombinant proteins through differential scanning microcalorimetry (DSC) to study a wide range of thermal transitions in biological systems, to determine melting temperatures as well as thermodynamic parameters associated to these changes.
- Kinetic analysis of protein - ligand interaction through Surface Plasmon Resonance (SPR) measurements, determination of kinetic association (kass) and dissociation (kdiss) constants.
- Determination of the hydrodynamic radius of macromolecules or particles through dynamic light scattering measurements coupled to size exclusion chromatography SEC-HPLC.