Differential scanning calorimetry (µDSC)

higher_order_structure

µDSC is an important and frequently used technique for the determination of the thermal stability of proteins.

µDSC is an important and frequently used technique for the determination of the thermal stability of proteins.

During µDSC analysis, the protein of interest is exposed to a temperature ramp, where the required thermal energy for each temperature increase is recorded in correlation to a reference sample (e.g., formulation buffer). As a result, protein unfolding events can be observed and the melting temperature (Tm) of each event can be determined. Also, the unfolding enthalpy (ΔH) of the protein or individual protein domains can be calculated from the area under the melting curve. µDSC is also employed to study the reversibility of unfolding events and can give insight into higher-order structures. µDSC is considered an “absolute technique”, as it does not rely on any reference standards to obtain quantitative results. However, µDSC requires much more time to analyze one sample than the orthogonal technique nanoDSF.

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Breitsprecher D., Glücklich N., Hawe A., Menzen T. "nanoDSF vs. µDSC: A Comparative Study for Biopharmaceutical Formulation Development" Whitepaper 2016

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