Since complex formation may be monitored in real time, it is possible to determine the kinetics of binding reactions. In this example the binding data were fit to a simple 1:1 interaction model. To confirm the validity of the biosensor method, the same interaction that was studied on the biosensor (top figure) was also analyzed in solution by stopped-flow fluorescence (bottom figure). The binding kinetics were shown to be identical from both techniques, illustrating that immobilization of one of the reactants onto the surface did not affect the reaction.

In general spr biosensors are able to resolve kinetics in the following ranges:
      ka = 100 to 1x108 M-1s-1
      kd = 1 to 1x10-6 s-1
for an overall affinity of:
      KD = 10 mM to 1 pM.

For more information on how biacore compares to solution-based techniques see:
Day et al., 2002 Protein Sci 11: 1017-1025.