Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 10, Issue 6, Pages 2752-2762Publisher
MDPI
DOI: 10.3390/ijms10062752
Keywords
titration calorimetry; enthalpy; protein-ligand binding; thermodynamics; carbonic anhydrase
Funding
- Lithuanian Science and Studies Foundation [N-06/09]
- Lithuanian Government
- EEA [2004-LT0019-IP-1EEE]
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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.
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