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Isothermal Microcalorimetry to Investigate Non Specific Interactions in Biophysical Chemistry

2009/07/28 by Vincent Ball, Clarisse Maechling · 1 citation
Biochemistry, Genetics and Molecular Biology · Chemistry · #Analytical Chemistry and Chromatography #Chemical physics #Chemistry #Computational chemistry #Enthalpy #Entropy (arrow of time) #Isothermal microcalorimetry #Isothermal titration calorimetry #Lipid Membrane Structure and Behavior #Molecule #Organic chemistry #Physical chemistry #Physics #Polyelectrolyte #Polymer #Supramolecular chemistry #Thermodynamics #thermodynamics and calorimetric analyses

paper · pdf · doi:10.3390/ijms10083283

openalex publication_date 2009/07/28 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30

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.

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