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Integrated Structural Biology Grenoble

Contact person(s) related to this article / Caroline Mas

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Studying macromolecules (and in particular proteins) by circular dichroism allows to obtain information about their folding. Circular dichroism (CD) spectroscopy measures differences in the absorption of left-handed polarized light versus right-handed polarized light which arise due to structural asymmetry. For proteins, far UV (180-260 nm) and near UV (250-330 nm) circular dichroism measurements give insight respectively into their secondary structure content and their tertiary organization.

Typical far UV spectra signature for α-helices, β-sheet and random coil

CD is particularly useful for monitoring changes in structure upon ligand binding or changes to the protein’s environment.

Thermal stability of folded molecules can be determined by performing temperature gradient to the sample. Similarly, conformational stability of a molecule and structural changes induced by complex formation can be checked at constant temperature by adding step by step chemical denaturation agents.


  • Estimation of protein and nucleic acid conformation (secondary and tertiary structure)
  • Determination of conformational changes (due to the interactions of asymmetric molecules) : Protein-protein interactions - Protein-DNA interactions - Protein-Ligand interactions - DNA-Ligand interactions
  • Determination of the thermodynamics of folding and unfolding of proteins and nucleic acids (thermal or chemical denaturation)
  • Kinetics of folding and unfolding of macromolecules

Key words

Secondary structure, tertiary organization, Interactions, Kinetics of folding and unfolding


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Professor Marc Jamin
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