Protein Crystallography and Biophysics Centre (BiophysX)
Institute of Structural and Molecular Biology (ISMB)
Birkbeck College / University College London

Differencial Scanning Calorimeter
(VP-DSC, Malvern)


Differential scanning calorimetry (DSC) enables accurate measurement of temperature dependent properties. The stability of a structure can be investigated, the melting temperature and the complete thermodynamics of melting can be determined.

Applications include the measurement or characterisation of
-    protein stability and folding,
-    the stability nucleic acids, membranes, lipids and micelles,
-    the effects of structural change on a molecule’s stability,
-    ultra-tight interactions (up to 1020 M-1),
-    other, pharmaceutical parameters.

Also for DSC, the solution conditions can be readily altered to allow determination of the pH or salt dependence of thermodynamic quantities. Alternatively, CD spectroscopy measures the melting of structures using their optical characteristics, and the Thermofluor Assay might serve as a much higher throughput method to screen various conditions.

Sample Requirements
  • Volume: 850 μl
  • Concentrations: depends on the protein, e.g. 0.1 mg/ml for lysozyme
  • Protein needs to be quite pure. A single band on an overloaded gel is a good indication

Buffer Requirements
  • Volume: 2 x 850 μl
  • Avoid buffers with pKa dependence on the temperature such as Tris
  • All reducing agents and particularly DTT are causing baseline artefacts. A test experiment is recommended
Brandts & Lin, Biochemistry 29, 6927-6940 (1990)
Gill et al, J. Biomol. Tech. 41(4), 167-193 (2010)

Please contact us for detailed protocols and planning your experiment.

ISMB Protein Crystallography and Biophysics Centre, Birkbeck, University of London
Last modified April 2021