title: Van't Hoff global analyses of variable temperature isothermal titration calorimetry data.
abstract: Isothermal titration calorimetry (ITC) can provide detailed information on the thermodynamics of biomolecular interactions in the form of equilibrium constants,KA, and enthalpy changes, ΔHA. A powerful application of this technique involves analyzing the temperature dependences of ITC-derivedKAand ΔHAvalues to gain insight into thermodynamic linkage between binding and additional equilibria, such as protein folding. We recently developed a general method for global analysis of variable temperature ITC data that significantly improves the accuracy of extracted thermodynamic parameters and requires no prior knowledge of the coupled equilibria. Here we report detailed validation of this method using Monte Carlo simulations and an application to study coupled folding and binding in an aminoglycoside acetyltransferase enzyme.
authors.affiliation: Department of Chemistry, McGill University, 801 Sherbrooke Street West, Montréal, Québec, Canada, H3A 2K6.
authors.forename: Lee A
authors.initials: LA
authors.lastname: Freiburger
authors.affiliation: Department of Chemistry, McGill University, 801 Sherbrooke Street West, Montréal, Québec, Canada, H3A 2K6.
authors.forename: Karine
authors.initials: K
authors.lastname: Auclair
authors.affiliation: Department of Chemistry, McGill University, 801 Sherbrooke Street West, Montréal, Québec, Canada, H3A 2K6.
authors.forename: Anthony K
authors.initials: AK
authors.lastname: Mittermaier
keywords: Aminoglycoside acetyltransferase; Coupled equilibria; Enthalpy; Heat capacity; Protein folding