Direct measurement of protein binding energetics by isothermal titration calorimetry

Stephanie Leavitt, Ernesto Freire

Research output: Contribution to journalReview articlepeer-review

516 Scopus citations


Of all the techniques that are currently available to measure binding, isothermal titration calorimetry is the only one capable of measuring not only the magnitude of the binding affinity but also the magnitude of the two thermodynamic terms that define the binding affinity: the enthalpy (ΔH) and entropy (ΔS) changes. Recent advances in instrumentation have facilitated the development of experimental designs that permit the direct measurement of arbitrarily high binding affinities, the coupling of binding to protonation/deprotonation processes and the analysis of binding thermodynamics in terms of structural parameters. Because isothermal titration calorimetry has the capability to measure different energetic contributions to the binding affinity, it provides a unique bridge between computational and experimental analysis. As such, it is increasingly becoming an essential tool in molecular design.

Original languageEnglish (US)
Pages (from-to)560-566
Number of pages7
JournalCurrent Opinion in Structural Biology
Issue number5
StatePublished - Sep 1 2001

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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