Calorimétrie à balayage de température

Determination de la thermostabilité (5-120 °C) de protéines, ADN, micelles grâce au VP-DSC. Détermination de la structure tertiaire et des interactions moléculaires.

A biomolecule in solution is in equilibrium between its native (folded) and denatured (unfolded) conformations. The higher the thermal transition midpoint (Tm), the more stable the molecule. DSC measures the enthalpy (∆H) of unfolding that results from heat-induced denaturation. It is also used to determine the change in heat capacity (ΔCp) of denaturation. DSC can elucidate the factors that contribute to the folding and stability of native biomolecules. These include hydrophobic interactions, hydrogen bonding, conformational entropy and the physical environment.

The precise and high quality data obtained from DSC provides vital information on protein stability in process development, and in the formulation of potential therapeutic candidates.

Macromolecules and macromolecular assemblies (>5000 Daltons), such as proteins, nucleic acids and lipids, can form well-defined structures that undergo thermally-induced conformational changes. These structural rearrangements result in the absorption of heat caused by the redistribution of non-covalent bonds. Differential scanning calorimeters measure this heat uptake.