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Protocols of IATC, DSC, and PPC: The Multistate Structural Transition of Cytochrome c

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Microcalorimetry of Biological Molecules

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

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Abstract

The recent development of high-precision calorimeters allows us to monitor the structural transition of biomolecules by calorimetry and thereby characterize the thermodynamic property changes accompanying three-dimensional structure changes. We developed isothermal acid-titration calorimetry (IATC) to evaluate the pH dependence of protein enthalpy. Using the double deconvolution method with precise differential scanning calorimetry (DSC), we revealed that the MG state is an equilibrium intermediate state of the reversible thermal three-state transition of the protein, and we successfully determined its volumetric properties by pressure perturbation calorimetry (PPC). Our findings underscore the importance of a precise calorimetry and analysis model for protein research.

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Author information

Authors and Affiliations

  1. Department of General Education, National Institute of Technology, Ube College, Ube, Japan

    Shigeyoshi Nakamura

  2. Department of Bioengineering, Nagaoka University of Technology, Nagaoka, Japan

    Shun-ichi Kidokoro

Authors
  1. Shigeyoshi Nakamura
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  2. Shun-ichi Kidokoro
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Corresponding author

Correspondence to Shun-ichi Kidokoro .

Editor information

Editors and Affiliations

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

    Eric Ennifar

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Nakamura, S., Kidokoro, Si. (2019). Protocols of IATC, DSC, and PPC: The Multistate Structural Transition of Cytochrome c. 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_2

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  • DOI: https://doi.org/10.1007/978-1-4939-9179-2_2

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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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