The PFBMI has an J-1500/ 450W 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 |
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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.
