​​

 

​

 

Microcalorimeters are used to study binding interactions between molecules, and conformational changes such as protein unfolding. Since microcalorimeters measure heat, microcalorimetry is considered a label-free quantification technique. Also, microcalorimeters do not require proteins and other biomaterials to be captured or immobilized.

​

Detection of heat change by microcalorimeters is non-optical and does not rely on measurements of fluorescence, so microcalorimeters can be used with essentially any naturally occurring protein or biopolymer materials. Applications range from confirming intended binding targets in small molecule drug discovery to the development of stable biologic drugs.

​

Microcalorimeters include two types of instruments: Isothermal Titration Calorimetry (ITC)  and Differential Scanning Calorimetry (DSC).