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Int J Mol Sci. 2009 Jun 18;10(6):2752-62. doi: 10.3390/ijms10062752.

Titration calorimetry standards and the precision of isothermal titration calorimetry data.

Author information

1
Laboratory of Biothermodynamics and Drug Design, Institute of Biotechnology, Vilnius, Lithuania. linami@ibt.lt

Abstract

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.

KEYWORDS:

carbonic anhydrase; enthalpy; protein-ligand binding; thermodynamics; titration calorimetry

PMID:
19582227
PMCID:
PMC2705514
DOI:
10.3390/ijms10062752
[Indexed for MEDLINE]
Free PMC Article

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