Related Experiment Video
Updated: Jun 16, 2026

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
Published on: September 7, 2011
Isothermal microcalorimetry to investigate non specific interactions in biophysical chemistry
Vincent Ball1,2, Clarisse Maechling3
1Institut National de la Santé et de la Recherche Médicale, Unité mixte de recherche 977, 11 rue Humann, 67085 Strasbourg Cédex, France.
Abstract:
Isothermal titration microcalorimetry (ITC) is mostly used to investigate the thermodynamics of "specific" host-guest interactions in biology as well as in supramolecular chemistry. The aim of this review is to demonstrate that ITC can also provide useful information about non-specific interactions, like electrostatic or hydrophobic interactions. More attention will be given in the use of ITC to investigate polyelectrolyte-polyelectrolyte (in particular DNA-polycation), polyelectrolyte-protein as well as protein-lipid interactions. We will emphasize that in most cases these "non specific" interactions, as their definition will indicate, are favoured or even driven by an increase in the entropy of the system. The origin of this entropy increase will be discussed for some particular systems. We will also show that in many cases entropy-enthalpy compensation phenomena occur.
Related Concept Videos
Calorimetry
Constant Pressure Calorimetry
Constant Volume Calorimetry
Noncovalent Attractions in Biomolecules
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
The Equilibrium Binding Constant and Binding Strength
The Equilibrium Binding Constant and Binding Strength

