Isothermal titration calorimetry.

Adrián Velázquez-Campoy, Hiroyasu Ohtaka, Azin Nezami, Salman Muzammil, Ernesto Freire

Research output: Contribution to journalReview articlepeer-review

Abstract

In the last two decades, isothermal titration calorimetry (ITC) has become the preferred technique to determine the binding energetics of biological processes, including protein-ligand binding, protein-protein binding, DNA-protein binding, protein-carbohydrate binding, protein-lipid binding, and antigen-antibody binding. In this unit several protocols are presented, ranging from the basic ones that are aimed at characterizing binding of moderate affinity to advanced protocols that are aimed at determining very high or very low affinity binding processes. Also, alternate protocols for special cases (homodimeric proteins and unstable proteins) and additional information accessible by ITC (heat capacity and protonation/deprotonation processes coupled to binding) are presented.

Original languageEnglish (US)
Pages (from-to)Unit 17.8
JournalCurrent protocols in cell biology / editorial board, Juan S. Bonifacino ... [et al.]
VolumeChapter 17
StatePublished - Sep 2004

ASJC Scopus subject areas

  • Cell Biology

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