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Microcalorimetry of Biological Molecules pp 33–44Cite as

Value of DSC in Characterization and Optimization of Protein Stability

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 1964))

Abstract

Differential scanning calorimetry (DSC) is a well-established technique for biomolecular stability studies. The technique is based on forced thermal denaturation of biomolecules in solution. Here we describe the use of DSC for characterization and optimization of stability of two proteins, a protein kinase and a mAb protein.

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Acknowledgments

The Sprint Bioscience AB (Huddinge, Sweden) is acknowledged for providing constructs of protein kinase.

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Authors and Affiliations

  1. Principal Scientist/Group Leader Analytical and Formulation Development, FUJIFILM Diosynth Biotechnologies U.S.A., Inc., Morrisville, NC, USA

    Katherine Bowers

  2. MicroCal, Malvern Panalytical, Uppsala, Sweden

    Natalia Markova

Authors
  1. Katherine Bowers
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  2. Natalia Markova
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Corresponding authors

Correspondence to Katherine Bowers or Natalia Markova .

Editor information

Editors and Affiliations

  1. Institut de Biologie Moléculaire et Cellulaire, Université de Strasbourg, CNRS, Strasbourg, France

    Eric Ennifar

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Bowers, K., Markova, N. (2019). Value of DSC in Characterization and Optimization of Protein Stability. In: Ennifar, E. (eds) Microcalorimetry of Biological Molecules. Methods in Molecular Biology, vol 1964. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9179-2_3

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  • DOI: https://doi.org/10.1007/978-1-4939-9179-2_3

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-9178-5

  • Online ISBN: 978-1-4939-9179-2

  • eBook Packages: Springer Protocols

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