Titration calorimetry standards and the precision of isothermal titration calorimetry data.
Current Isothermal Titration Calorimetry (ITC) data in the literature have relatively high errors in the measured enthalpies of protein-ligand binding reactions. There is a need for universal validation standards for titration calorimeters. Several inorganic salt co-precipitation and buffer protonation reactions have been suggested as possible enthalpy standards. The performances of several commercial calorimeters, including the VP-ITC, ITC200, and Nano ITC-III, were validated using these suggested standard reactions.
Baranauskienė
Lina
L
Laboratory of Biothermodynamics and Drug Design / Institute of Biotechnology, Graičiūno 8, Vilnius, LT-02241, Lithuania.
Petrikaitė
Vilma
V
Laboratory of Biothermodynamics and Drug Design / Institute of Biotechnology, Graičiūno 8, Vilnius, LT-02241, Lithuania.
Matulienė
Jurgita
J
Laboratory of Biothermodynamics and Drug Design / Institute of Biotechnology, Graičiūno 8, Vilnius, LT-02241, Lithuania.
Matulis
Daumantas
D
Laboratory of Biothermodynamics and Drug Design / Institute of Biotechnology, Graičiūno 8, Vilnius, LT-02241, Lithuania.
D002021:Buffers; D002151:Calorimetry / Q000592:standards*; D024402:Carbonic Anhydrase II / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D013696:Temperature; D013816:Thermodynamics
D002021:Buffers; D008024:Ligands; D011506:Proteins; D011994:Recombinant Proteins; D024402:Carbonic Anhydrase II