Thermodynamic Characterisation

Characterizing the thermodynamics of molecular interactions complements protein structural information by providing a more complete understanding of the forces that lead to complex formation. Although isothermal titration calorimetry (ITC) is the standard method for direct measurement of binding thermodynamics, high sample consumption and low solubility can limit its application in some systems. As an alternative approach, optical biosensor interaction technology such as Biacore offers an opportunity to measure the temperature dependence of binding constants and determine thermodynamics with significantly lower sample requirements.
(I. Navratilova et.al, Analytical Biochemistry, Volume 364, Issue 1, 1 May 2007, P. 67-7)

Enthalpy and entropy are measured using the Van’t Hoff method and calculated from affinities measured for the interaction over the temperature range 4-40 °C.