Cooperativity in Binding Processes: New Insights from Phenomenological Modeling.

ABSTRACT: Cooperative binding is one of the most interesting and not fully understood phenomena involved in control and regulation of biological processes. Here we analyze the simplest phenomenological model that can account for cooperativity (i.e. ligand binding to a macromolecule with two binding sites) by generating equilibrium binding isotherms from deterministically simulated binding time courses. We show that the Hill coefficients determined for cooperative binding, provide a good measure of the Gibbs free energy of interaction among binding sites, and that their values are independent of the free energy of association for empty sites. We also conclude that although negative cooperativity and different classes of binding sites cannot be distinguished at equilibrium, they can be kinetically dif

SUBMITTER: Cattoni DI 

PROVIDER: S-EPMC4696654 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature