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Calorimetry is the science of measuring heat changes from chemical reactions or physical events.

Calorimetry relies on the fact that all chemical reactions involve a change in energy, usually accompanied by heat release (exothermic) or absorption (endothermic). Microcalorimetry is an ultrasensitive development of the technique that measures very small heat changes in small sample volumes, making it suitable for biomaterials.

Microcalorimetry is used to study reactions involving biomolecules, including interactions between molecules and conformational changes such as protein folding. Applications range from confirming intended binding targets in small molecule drug discovery to the development of stable biotherapeutics.

These processes are often studied using two calorimetric techniques: Isothermal Titration Calorimetry (ITC) and Differential Scanning Calorimetry (DSC).

Isothermal Titration Calorimetry (ITC)

Isothermal Titration Calorimetry (ITC) is used to study the binding behavior of biomolecules. It is an essential tool for drug design and the study and regulation of protein interactions.

ITC directly measures the heat released or absorbed during a biomolecular binding event. This allows accurate determination of binding constants (KD), reaction stoichiometry (n), enthalpy (∆H), and entropy (ΔS).

ITC is used for:

  • Quantify binding affinity.
  • Candidate selection and optimization.
  • Measurement of thermodynamics and active concentration.
  • Characterization of mechanism of action.
  • Confirmation of intended binding targets in small molecule drug discovery.
  • Determination of binding specificity and stoichiometry.
  • Validation of IC50 and EC50 values during hit-to-lead.
  • Measurement of enzyme kinetics.

Differential Scanning Calorimetry (DSC)

Differential Scanning Calorimetry (DSC) is a technique for understanding the stability of proteins and other biomolecules. It has wide application in protein engineering, rational drug design and biopharmaceutical production, where developing stable proteins is a critical goal.

DSC is a key thermal analysis technique that measures heat changes that occur in the biomolecule during a controlled increase or decrease in temperature, making it possible to study materials in their native state.

DSC enables:

  • Characterization and selection of the most stable proteins/potential candidates in biotherapeutic development.
  • Ligand interaction studies.
  • Rapid optimization of purification and manufacturing conditions.
  • Easy, rapid determination of optimum conditions for liquid formulations.
  • Quick stability-indicating assay for target proteins for use in screening.

Related products

MicroCal range Microcalorimeters for characterization of biomolecular stability and interactions MicroCal Range
Microcalorimetry, Label-free analysis
Temperature range
-10°C to 130°C
Sample throughput
2per 8h day to 50per 24h day
Isothermal Titration Calorimetry, Differential Scanning Calorimetry
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Using Isothermal Titration Calorimetry to support the development of therapeutic enzymes Webinar - Live (English)

This webinar will describe the use of Isothermal Titration Calorimetry (ITC) to establish the enzymatic properties of a lysosomal enzyme with potential therapeutic value. The technique was used by the team at Swedish Orphan Biovitrum (Sobi) to enable...

MicroCal ITC range
October 26 2016

The Power of Heat: Digging Deeper with Differential Scanning Calorimetry to Study Key Protein Characteristics Webinar - Recorded (English)

Differential Scanning Calorimetry (DSC) has a long history of playing a vital role in biopharmaceutical development. From candidate selection to formulation development, stability monitoring and bio-similarity assessment, DSC remains one of the top a...

MicroCal DSC range
Date recorded:
August 16 2016

Characterization of biopharmaceutical stability with Differential Scanning Calorimetry: Preformulation and formulation development Whitepaper (English)

DSC is an established analytical tool used during preformulation and formulation development of biopharmaceuticals. Rank ordering of thermal transition midpoint (TM) by DSC is commonly used to screen formulation buffers, pH and excipients.  Typicalll...

Characterization of biopharmaceutical stability with Differential Scanning Calorimetry: Candidate selection for developability Whitepaper (English)

Biopharmaceutical proteins are characterized and optimized for stability throughout development. Differential scanning calorimetry (DSC) is a key biophysical assay used to rank order thermal stability. This white paper discusses how DSC is used to se...

Using DSC to characterize thermotropic phase transitions in lipid bilayer membranes Application Note (English)

Liposomes have been widely used as model membranes and in drug delivery, as their basic properties can easily be varied to target desired properties (lipid composition, concentration, water content, media (different buffers, varying ionic strength, p...

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Using Isothermal Titration Calorimetry to support the development of therapeutic enzymes
(October 26 2016)

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