All chemical reactions or physical events involve a change in energy, usually accompanied by heat release (exothermic) or absorption (endothermic). Calorimetry is the science of measuring heat changes from chemical reactions or physical events. Microcalorimetry is an ultrasensitive development of the technique that measures very small heat changes in small sample volumes, making it suitable for biomaterials.
Malvern MicroCal microcalorimeters are powerful, analytical tools used to study characterization of biomolecular stability and interactions. The range includes both Isothermal Titration and Differential Scanning calorimetry.

How it works

Isothermal Titration calorimetry

Isothermal Titration Calorimetry (ITC) is a technique used in quantitative studies of a wide variety of biomolecular interactions. It works by directly measuring the heat that is either released or absorbed during a biomolecular binding event.
This allows accurate determination of binding parameters:

• affinity constants (K_D)
• stoichiometry (n)
• enthalpy (∆H)
• entropy (ΔS)
  
  

Differential Scanning Calorimetry

Differential Scanning Calorimetry (DSC) is a technique used to characterize the stability of a protein or other biomolecule directly in its native form. It does this by measuring the heat change associated with the molecule’s thermal denaturation when heated at a constant rate.
This allows accurate determination of “unfolding” parameters:

• Heat capacity change  (∆C_p)
• Temperature midpoint (T_m)
• Enthalpy  (∆H)