Ligand-induced thermostability in proteins: Thermodynamic analysis of ANS-albumin interaction

A comparative thermodynamic study of the interaction of anilinonaphthalene sulfonate (ANS) derivatives with bovine serum albumin (BSA) was performed by using differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC). The chemically related ligands, 1,8-ANS and 2,6-ANS, prese...

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Detalles Bibliográficos
Autores principales:	Celej, M.S., Dassie, S.A., Freire, E., Bianconi, M.L., Fidelio, G.D.
Formato:	JOUR
Materias:	ANS derivative Linked equilibria Protein stability Protein unfolding thermodynamics Protein-ligand interaction 8 anilino 1 naphthalenesulfonic acid albumin article binding affinity differential scanning calorimetry electricity energy transfer entropy force hydrophobicity isothermal titration calorimetry mathematical computing priority journal protein conformation protein domain protein interaction simulation thermodynamics thermography thermostability validation process Anilino Naphthalenesulfonates Animals Calorimetry, Differential Scanning Cattle Heat Kinetics Ligands Models, Molecular Protein Binding Protein Denaturation Protein Folding Serum Albumin, Bovine Thermodynamics Bovinae
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_15709639_v1750_n2_p122_Celej
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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