How does DSC work?
Differential Scanning Calorimetry (DSC) is a powerful analytical tool which directly measures the stability and unfolding of a protein, lipid, or nucleic acid. In DSC, the biomolecule is heated at a constant rate and there is a detectable heat change associated with thermal denaturation. In a single DSC experiment, can determine: • Transition midpoint – Tm • Enthalpy (ΔH) and heat capacity change (ΔCp) associated with unfolding A biomolecule in aqueous solution is in equilibrium between the native (folded) conformation and its denatured (unfolded) conformation. The stability of the native state is based on the magnitude of the Gibbs free energy (ΔG) of the system and the thermodynamic relationships between enthalpy (ΔH) and entropy (ΔS) changes. A positive ΔG indicates the native state is more stable than the denatured state – the more positive the ΔG, the greater the stability. For a protein to unfold, stabilizing forces need to be broken. Conformational entropy overcomes stabilizing
