Protocol

Protein-Ligand Interactions

Volume 305 of the series Methods in Molecular Biology™ pp 1-15

Isothermal Titration Calorimetry

  • Edwin A. LewisAffiliated withDepartment of Chemistry and Biochemistry, Northern Arizona University
  • , Kenneth P. MurphyAffiliated withDepartment of Biochemistry, University of Iowa

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Abstract

Isothermal titration calorimetry is an ideal technique for measuring biological binding interactions. It does not rely on the presence of chromophores or fluorophores, nor does it require an enzymatic assay. Because the technique relies only on the detection of a heat effect upon binding, it can be used to measure the binding constant, K, the enthalpy of binding, ΔH° and the stoichiometry, or number of binding sites, n. This chapter describes instrumentation, experimental design, and the theoretical underpinnings necessary to run and analyze a calorimetric binding experiment.

Key Words

Binding thermodynamics proton linkage enthalpy heat capacity data analysis