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Differential Scanning Calorimetry (DSC)


Differential Scanning Calorimetry (DSC) measures enthalpy (ΔH) of protein unfolding due to heat denaturation. A protein in solution is in equilibrium between the native (folded) conformation and its denatured (unfolded) state. The higher the transition midpoint (Tm) when 50% of the protein molecules are unfolded, the more stable the protein. DSC 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 proteins, including hydrophobic interactions, hydrogen bonding, conformational entropy, and the physical environment.


The VP-DSC is a highly sensitive, easy-to-use differential scanning calorimeter for the study of proteins in solution without the need for labelling. It can provide fast and accurate transition midpoint (Tm) determination to understand the factors that affect the conformation and stability of a protein of interest.

The VP-DSC is controlled by VPViewer software and data analysis is performed with MicroCal-enabled Origin software. Other features include:

  • Can be used with solutions that interfere with optical methods including turbid or colored solutions or particulate suspensions.
  • Provides insights into mechanisms of unfolding and refolding.
  • Minimal assay development needed.




Instrument use (independent use)

$5/hr up to $50/day



*Cost of instrument time + $50/hr Facility Manager time



Booking Calendar: Book Here



Botterell Hall, Room 667



If you have any questions please contact Xiaohu Yan at