000168018 001__ 168018
000168018 005__ 20260127151102.0
000168018 0248_ $$2sideral$$a57981
000168018 037__ $$aART-2006-57981
000168018 041__ $$aeng
000168018 100__ $$0(orcid)0000-0001-5702-4538$$aVelazquez Campoy,Adrian$$uUniversidad de Zaragoza
000168018 245__ $$aExact analysis of heterotropic interactions in proteins: Characterization of cooperative ligand binding by isothermal titration calorimetry
000168018 260__ $$c2006
000168018 5060_ $$aAccess copy available to the general public$$fUnrestricted
000168018 5203_ $$aIntramolecular interaction networks in proteins are responsible for heterotropic ligand binding cooperativity, a biologically important, widespread phenomenon in nature (e.g., signaling transduction cascades, enzymatic cofactors, enzymatic allosteric activators or inhibitors, gene transcription, or repression). The cooperative binding of two (or more) different ligands to a macromolecule is the underlying principle. To date, heterotropic effects have been studied mainly kinetically in enzymatic systems. Until now, approximate approaches have been employed for studying equilibrium heterotropic ligand binding effects, except in two special cases in which an exact analysis was developed: independent binding (no cooperativity) and competitive binding (maximal negative cooperativity). The exact analysis and methodology for characterizing ligand binding cooperativity interactions in the general case (any degree of cooperativity) using isothermal titration calorimetry are presented in this work. Intramolecular interaction pathways within the allosteric macromolecule can be identified and characterized using this methodology. As an example, the thermodynamic characterization of the binding interaction between ferredoxin-NADP1 reductase and its three substrates, NADP1, ferredoxin, and flavodoxin, as well as the characterization of their binding cooperativity interaction, is presented.
000168018 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttps://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
000168018 590__ $$a4.757$$b2006
000168018 591__ $$aBIOPHYSICS$$b8 / 66 = 0.121$$c2006$$dQ1$$eT1
000168018 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000168018 700__ $$0(orcid)0000-0003-4010-849X$$aGoni,Guillermina
000168018 700__ $$aPeregrina,Jose Ramon$$uUniversidad de Zaragoza
000168018 700__ $$0(orcid)0000-0001-8743-0182$$aMedina,Milagros$$uUniversidad de Zaragoza
000168018 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000168018 773__ $$g91, 5 (2006), 1887-1904$$pBiophys. j.$$tBIOPHYSICAL JOURNAL$$x0006-3495
000168018 8564_ $$s1001667$$uhttps://zaguan.unizar.es/record/168018/files/texto_completo.pdf$$yPostprint
000168018 8564_ $$s687922$$uhttps://zaguan.unizar.es/record/168018/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint
000168018 909CO $$ooai:zaguan.unizar.es:168018$$particulos$$pdriver
000168018 951__ $$a2026-01-27-15:07:31
000168018 980__ $$aARTICLE