Differential Scanning Calorimetry to Quantify Heat-Induced Aggregation in Concentrated Protein Solutions

Matthew R. Jacobs, Mark Grace, Alice Blumlein, Jennifer J. McManus*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter in a book

9 Citations (Scopus)


Differential scanning calorimetry (DSC) is an important technique to measure the thermodynamics of protein unfolding (or folding). Information including the temperature for the onset of unfolding, the melt transition temperature (Tm), enthalpy of unfolding (ΔH), and refolding index (RI) are useful for evaluating the heat stability of proteins for a range of biochemical, structural biology, industrial, and pharmaceutical applications. We describe a procedure for careful sample preparation of proteins for DSC measurements and data analysis to determine a range of thermodynamic parameters. In particular, we highlight a measure of protein refolding following complete thermal denaturation (RI), which quantifies the proportion of protein lost to irreversible aggregation after thermal denaturation.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages13
Publication statusPublished - 1 Jan 2019

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029


  • Differential scanning calorimetry
  • Enthalpy
  • Melt transition temperature
  • Protein aggregation
  • Refolding index
  • Thermal denaturation


Dive into the research topics of 'Differential Scanning Calorimetry to Quantify Heat-Induced Aggregation in Concentrated Protein Solutions'. Together they form a unique fingerprint.

Cite this