Handling complexity in biological interactions

Abstract

Biological processes rely on interactions between many binding partners. Binding results in the modulation of the conformational landscape of the interacting molecules, a phenomenon rooted in folding and binding cooperativity underlying the allosteric functional regulation of biomacromolecules. The conformational equilibrium of a protein and the binding equilibria of different interacting and cooperative ligands are coupled giving rise to a complex scenario in which protein function can be finely tuned and modulated. Binding cooperativity and allostery add additional levels of complexity in protein function regulation. Here we will review some important concepts associated with binding, cooperativity and allostery in protein interactions, illustrated with several representative protein-dependent biological systems related to drug discovery and physiological mechanisms characterization and studied by isothermal titration calorimetry.