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Isothermal Titration Calorimetry/Evidence
Method evidence record

Isothermal Titration Calorimetry

Isothermal Titration Calorimetry (ITC) is a thermodynamic technique that measures heat released or absorbed during biomolecular binding events at constant temperature. Developed by Wiseman and colleagues in 1989, ITC directly determines binding affinity (Kd), enthalpy (ΔH), and entropy (ΔS) in a single experiment, making it one of the most comprehensive methods for characterizing molecular interactions without requiring labels or immobilization.

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Source record

Citations copied verbatim from the method’s source record. No claim-level verification is inferred from them.

Isothermal Titration Calorimetry
Taxonomic method record · process-pipeline / spectroscopy
  • Wiseman, T., Williston, S., Brandts, J. F., & Lin, L. N. (1989). Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Analytical Biochemistry, 179(1), 131-137. · DOI 10.1016/0003-2697(89)90213-3
  • Garbett, N. C., & Chaires, J. B. (2012). Binding: A statistical thermodynamic model. Biophysical Journal, 86(6), 3493-3494. · URL
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Related methods

Generated from the method graph and shown as machine-suggested relations — no evidence claim is inferred.

Same method familyCircular Dichroismmachine-suggested · Relational suggestion, not evidence.Same method familyElectron Paramagnetic Resonancemachine-suggested · Relational suggestion, not evidence.Same method familySurface Plasmon Resonancemachine-suggested · Relational suggestion, not evidence.

Evidence status

Sources recorded, not reviewed

Bibliographic sources are present. Claim-level evidence review has not been performed.

Sources

2 recorded citations, copied from the method source record.

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