Thermodynamic information about complex formation can be obtained by analyzing the same interaction at different temperatures. This example shows the binding profiles for the same concentrations of analyte injected over the same surface at 5, 15, 25 and 35 degrees C. It is easy to see the effect temperature has on increasing the dissociation rate of the complex and thereby weakening the overall affinity. Information about the enthalpic and entropic driving forces for complex formation, as well as the transition state, can be obtained from van’t Hoff and Eyring plots of the temperature-dependent binding constants.

The ability to analyze binding reactions at different temperatures is also beneficial from a practical standpoint. In many systems the immobilized component is more stable at a lower temperature and therefore easier to analyze. In other cases, it's often important to collect binding constants at physiological temperature.

For more information on how biacore has been used to measure thermodynamic parameters see:
Day et al., 2002 Protein Sci 11: 1017-1025.