Titration calorimetry standards and the precision of isothermal titration calorimetry data

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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Buffers
  • Calorimetry / standards*
  • Carbonic Anhydrase II / chemistry
  • Carbonic Anhydrase II / genetics
  • Carbonic Anhydrase II / metabolism
  • Hydrogen-Ion Concentration
  • Ligands
  • Protein Binding
  • Proteins / chemistry
  • Proteins / metabolism
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Temperature
  • Thermodynamics

Substances

  • Buffers
  • Ligands
  • Proteins
  • Recombinant Proteins
  • Carbonic Anhydrase II