title: Studying the allosteric energy cycle by isothermal titration calorimetry.
abstract: Isothermal titration calorimetry (ITC) is a powerful biophysical technique which allows a complete thermodynamic characterization of protein interactions with other molecules. The possibility of dissecting the Gibbs energy of interaction into its enthalpic and entropic contributions, as well as the detailed additional information experimentally accessible on the intermolecular interactions (stoichiometry, cooperativity, heat capacity changes, and coupled equilibria), make ITC a suitable technique for studying allosteric interactions in proteins. Two experimental methodologies for the characterization of allosteric heterotropic ligand interactions by ITC are described in this chapter, illustrated with two proteins with markedly different structural and functional features: a photosynthetic electron transfer protein and a drug target viral protease.
authors: Institute of Biocomputation and Physics of Complex Systems (BIFI), Universidad de Zaragoza, Zaragoza, Spain. mmartine@unizar.es
authors: Marta
authors: M
authors: Martinez-Julvez
authors: Olga
authors: O
authors: Abian
authors: Sonia
authors: S
authors: Vega
authors: Milagros
authors: M
authors: Medina
authors: Adrian
authors: A
authors: Velazquez-Campoy
mesh_terms: D000494:Allosteric Regulation / Q000502:physiology; D002151:Calorimetry / Q000379:methods*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D011506:Proteins