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Updated: Jun 17, 2026

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
Published on: November 21, 2017
Thermal melting studies of ligand DNA interactions
Aurore Guédin1, Laurent Lacroix, Jean-Louis Mergny
1Equipe Santé, Laboratoire Régulation et Dynamique des Génomes, Muséum National d'Histoire Naturelle USM 503, INSERM UR 565, CNRS UMR 5153, Paris, France.
Abstract:
A simple thermal melting experiment may be used to demonstrate the stabilization of a given structure by a ligand (usually a small molecule, sometimes a peptide). Preparation of the sample is straightforward, and the experiment itself requires an inexpensive apparatus. Furthermore, reasonably low amounts of sample are required. A qualitative analysis of the data is simple: An increase in the melting temperature (T(m)) indicates preferential binding to the folded form as compared to the unfolded form. However, it is perilous to derive an affinity constant from an increase in T(m) as other factors play a role.
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