000061356 001__ 61356
000061356 005__ 20210121114510.0
000061356 0247_ $$2doi$$a10.1016/j.ymeth.2014.09.010
000061356 0248_ $$2sideral$$a89846
000061356 037__ $$aART-2015-89846
000061356 041__ $$aeng
000061356 100__ $$0(orcid)0000-0002-1232-6310$$aVega, S.
000061356 245__ $$aA unified framework based on the binding polynomial for characterizing biological systems by isothermal titration calorimetry
000061356 260__ $$c2015
000061356 5060_ $$aAccess copy available to the general public$$fUnrestricted
000061356 5203_ $$aIsothermal titration calorimetry (ITC) has become the gold-standard technique for studying binding processes due to its high precision and sensitivity, as well as its capability for the simultaneous determination of the association equilibrium constant, the binding enthalpy and the binding stoichiometry. The current widespread use of ITC for biological systems has been facilitated by technical advances and the availability of commercial calorimeters. However, the complexity of data analysis for non-standard models is one of the most significant drawbacks in ITC. Many models for studying macromolecular interactions can be found in the literature, but it looks like each biological system requires specific modeling and data analysis approaches. The aim of this article is to solve this lack of unity and provide a unified methodological framework for studying binding interactions by ITC that can be applied to any experimental system. The apparent complexity of this methodology, based on the binding polynomial, is overcome by its easy generalization to complex systems.
000061356 536__ $$9info:eu-repo/grantAgreement/ES/DGA/B01$$9info:eu-repo/grantAgreement/ES/DGA/B89$$9info:eu-repo/grantAgreement/ES/FIS/PI10-00186$$9info:eu-repo/grantAgreement/ES/ISCIII/CP07-00289$$9info:eu-repo/grantAgreement/ES/MICINN/BFU2010-19451$$9info:eu-repo/grantAgreement/ES/MICINN/PTA2009-2341-I
000061356 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
000061356 590__ $$a3.503$$b2015
000061356 591__ $$aBIOCHEMICAL RESEARCH METHODS$$b18 / 77 = 0.234$$c2015$$dQ1$$eT1
000061356 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b99 / 289 = 0.343$$c2015$$dQ2$$eT2
000061356 592__ $$a2.367$$b2015
000061356 593__ $$aMolecular Biology$$c2015$$dQ1
000061356 593__ $$aBiochemistry, Genetics and Molecular Biology (miscellaneous)$$c2015$$dQ1
000061356 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000061356 700__ $$0(orcid)0000-0001-5664-1729$$aAbian, O.
000061356 700__ $$0(orcid)0000-0001-5702-4538$$aVelazquez-Campoy, A.$$uUniversidad de Zaragoza
000061356 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000061356 773__ $$g76 (2015), 99-115$$pMethods$$tMETHODS$$x1046-2023
000061356 8564_ $$s620182$$uhttps://zaguan.unizar.es/record/61356/files/texto_completo.pdf$$yPostprint
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000061356 951__ $$a2021-01-21-10:56:15
000061356 980__ $$aARTICLE