Fitting two- and three-site binding models to isothermal titration calorimetric data.

ABSTRACT: As isothermal titration calorimetry (ITC) gains popularity for the characterization of enthalpies and equilibrium association constants of simple 1:1 biomolecular interactions, its use for more complex systems is growing. The method is increasingly used to study interactions in which a single binding partner (molecule "A") interacts with multiple copies of a second partner ("B"); thus examinations of ABB and ABBB interactions are not uncommon. The structure of ITC data (commonly formatted as isotherms) has a strong bearing on the ability of the researcher to extract the necessary parameters from them. Usually, only 10-30 injections are recorded in a single ITC experiment. Even if replicates are performed, the data must support the extraction of up to twelve parameters from an ABBB system.

SUBMITTER: Brautigam CA 

PROVIDER: S-EPMC4591754 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature