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

  • Shigeyoshi Nakamura
  • Shun-ichi KidokoroEmail author
Part of the Methods in Molecular Biology book series (MIMB, volume 1964)


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.

Key words

Differential scanning calorimetry Pressure perturbation calorimetry Cytochrome c Isothermal acid-titration calorimetry 


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© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Department of General EducationNational Institute of Technology, Ube CollegeUbeJapan
  2. 2.Department of BioengineeringNagaoka University of TechnologyNagaokaJapan

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