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Isothermal Titration Calorimetry

Abstract

Calorimetry is a classical biophysical method that by definition measures heat. In isothermal titration calorimetry (ITC), the heat is the result of titrating interacting components together and allows direct determination of the thermodynamics for this process. The measured heat reflects the enthalpy change (Delta H), and the prospect of determining this in biological systems where high-resolution structural information is available has led to the possibility of rational thermodynamics-guided design of ligands. Although there are limitations to this approach due to the participation of solvent in the thermodynamics, ITC has become an established technique in many labs providing a valuable tool with which to quantify protein-protein interactions. With careful use, ITC can also provide additional insights into the binding process or be used in increasingly complex systems and where interaction is coupled to other molecular events.

article Article; Book Chapter
date_range 2021
language English
link Link of the paper
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Featured Keywords

Isothermal titration calorimetry
ITC
Thermodynamics
Enthalpy
Entropy
Free energy
Dissociation constant
Heat capacity
Stoichiometry
Binding affinity
Binding kinetics
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