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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Equipment

Circular Dichroism

Scientific Fields
Diseases
Organisms
Applications
Technique

AVIV • 215

The PFBMI has an Aviv 215 instrument with accessories for the measurement of total fluorescence and to perform titrations. Studying macromolecules (and in particular proteins) by circular dichroism allows to obtain information about their folding. 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. The thermal stability of folding can be determined by applying a temperature gradient to the sample. Similarly, it is possible to quantify the conformational stability of a molecule at constant temperature or the structural changes induced by the formation of a complex, by performing a titration, respectively by a denaturing agent or a ligand.

Circular dichroism in the near UV  Circular dichroism in the far UV 

Thermal stability of folded molecules can be determined by performing temperature scans. 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 denaturating agents or specific ligands using a computer driven titrator.