Theoretical aspects of the quantitative characterization of ligand binding.

Living organisms grow, differentiate, reproduce, and respond to their environment via specific and integrated interactions between biomolecules. The investigation of molecular interactions therefore constitutes a major area of biochemical study, occupying a ubiquitous and central position between molecular physiology on the one hand and structural chemistry on the other. While specificity resides in the details of structural recognition, the dynamic interplay between biomolecules is orchestrated precisely by the thermodynamics of the biomolecular equilibria involved. A common set of physicochemical principles applies to all such phenomena, irrespective of whether the interaction of interest involves an enzyme and its substrate or inhibitor, a hormone or growth factor and its receptor, an antibody and its antigen, or, indeed, the binding of effector molecules that modulate these interactions. The binding affinity, binding specificity, number of binding sites per molecule, as well as the enthalpic and entropic contributions to the binding energy are common parameters that assist an understanding of the biochemical outcome. This unit aims to provide an overview of the design and interpretation of binding experiments.