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

1 Citation (Scopus)

Abstract

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.
Pages117-129
Number of pages13
DOIs
Publication statusPublished - 1 Jan 2019

Publication series

NameMethods in Molecular Biology
Volume2039
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Keywords

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

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