A methodology using biosensor technology for combined kinetic and thermodynamic
analysis of biomolecular interactions is described. Rate and affinity constants are …

Publisher Summary This chapter reviews that the popularity of using biosensors to
characterize biomolecular interactions continues to grow. These instruments are capable of …

The introduction of affinity-based biosensors has permitted label-free functional analysis of
biomolecular interactions in real time. A variety of methods are now based on BIACORE® …

Microcalorimetry can be used to determine directly the energetics and stoichiometry of
macromolecular interactions by detecting the heat energy changes that, in most …

Publisher Summary The chapter demonstrates the potential of the thermodynamic approach
based on high sensitivity scanning calorimetry measurements to provide quantitative energy …

The interaction of two molecules binding to each other is described by two rate parameters,
the association rate parameter ka and the dissociation rate parameter kd. Under …

A procedure for evaluating the thermodynamic equilibrium constant by kinetic analysis of
sensorgrams which deviate from the pseudo-first-order kinetic behavior predicted for 1: 1 …

Whereas the concentration of a biomolecule simply refers to the amount of chemical
substance per unit of volume, its active concentration refers to a relational parameter that …

The theory of a method for determining active concentration of nonpurified protein samples
using the BIAcore biosensor technology has been developed. The method relies on change …

Isothermal titration calorimetry (ITC) is perhaps the most rigorous commercially available
method for characterizing protein‐ligand interactions. In this method, interactions are …