title: A unified framework based on the binding polynomial for characterizing biological systems by isothermal titration calorimetry.
abstract: Isothermal titration calorimetry (ITC) has become the gold-standard technique for studying binding processes due to its high precision and sensitivity, as well as its capability for the simultaneous determination of the association equilibrium constant, the binding enthalpy and the binding stoichiometry. The current widespread use of ITC for biological systems has been facilitated by technical advances and the availability of commercial calorimeters. However, the complexity of data analysis for non-standard models is one of the most significant drawbacks in ITC. Many models for studying macromolecular interactions can be found in the literature, but it looks like each biological system requires specific modeling and data analysis approaches. The aim of this article is to solve this lack of unity and provide a unified methodological framework for studying binding interactions by ITC that can be applied to any experimental system. The apparent complexity of this methodology, based on the binding polynomial, is overcome by its easy generalization to complex systems.
authors.affiliation: Institute of Biocomputation and Physics of Complex Systems (BIFI), Joint Unit IQFR-CSIC-BIFI, Universidad de Zaragoza, Zaragoza, Spain.
authors.forename: Sonia
authors.initials: S
authors.lastname: Vega
authors.affiliation: Institute of Biocomputation and Physics of Complex Systems (BIFI), Joint Unit IQFR-CSIC-BIFI, Universidad de Zaragoza, Zaragoza, Spain; Instituto Aragonés de Ciencias de la Salud (IACS), Zaragoza, Spain; IIS Aragón, Zaragoza, Spain; Centro de Investigación Biomédica en Red en el Área Temática de Enfermedades Hepáticas y Digestivas (CIBERehd), Spain. Electronic address: oabifra@unizar.es.
authors.forename: Olga
authors.initials: O
authors.lastname: Abian
authors.affiliation: Institute of Biocomputation and Physics of Complex Systems (BIFI), Joint Unit IQFR-CSIC-BIFI, Universidad de Zaragoza, Zaragoza, Spain; Department of Biochemistry and Molecular and Cell Biology, University of Zaragoza, Zaragoza, Spain; Fundacion ARAID, Government of Aragon, Spain. Electronic address: adrianvc@unizar.es.
authors.forename: Adrian
authors.initials: A
authors.lastname: Velazquez-Campoy
mesh_terms: D001665:Binding Sites; D002118:Calcium / Q000737:chemistry; D002151:Calorimetry / Q000379:methods*; D002352:Carrier Proteins / Q000737:chemistry; D004492:Edetic Acid / Q000737:chemistry; D047908:Intracellular Signaling Peptides and Proteins; D008024:Ligands; D013816:Thermodynamics; D017361:Viral Nonstructural Proteins / Q000737:chemistry; D012697:Serine Endopeptidases; D043583:Nucleoside-Triphosphatase; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases
chemical_list: D002118:Calcium; D002352:Carrier Proteins; D004492:Edetic Acid; D047908:Intracellular Signaling Peptides and Proteins; D008024:Ligands; D017361:Viral Nonstructural Proteins; C084422:NS3 protein, hepatitis C virus; D012697:Serine Endopeptidases; D043583:Nucleoside-Triphosphatase; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases; C455041:NS4A cofactor peptide, Hepatitis C virus
keywords: Allosteric and polysteric linkage; Binding polynomial; Homotropic and heterotropic chemical linkage; Isothermal titration calorimetry; Ligand binding; Macromolecular interactions