IATC, DSC, and PPC Analysis of Reversible and Multistate Structural Transition of Cytochrome c

Development of precise calorimeters has enabled us to monitor the structural transition of biomolecules by calorimetry to characterize the thermodynamic property changes accompanying three-dimensional structure change. We developed isothermal acid-titration calorimetry to evaluate the pH dependence...

Full description

Saved in:
Bibliographic Details
Published inMethods in enzymology Vol. 567; p. 391
Main Authors Kidokoro, Shun-ichi, Nakamura, Shigeyoshi
Format Journal Article
LanguageEnglish
Published United States 01.01.2016
Subjects
Calorimetry - methods
Cytochromes c - metabolism
Protein Folding
Thermodynamics
Intermediate state
Gibbs free energy
Stability
Proton binding number
Enthalpy
Heat capacity
Entropy
Partial specific volume
Folding/unfolding
Molten globule
Online AccessGet more information

Cover

More Information
Summary:Development of precise calorimeters has enabled us to monitor the structural transition of biomolecules by calorimetry to characterize the thermodynamic property changes accompanying three-dimensional structure change. We developed isothermal acid-titration calorimetry to evaluate the pH dependence of protein enthalpy, and demonstrated the thermodynamic transition between the native and molten globule (MG) states of cytochrome c with very small enthalpy change (~20 kJ/mol) by this method. The double deconvolution method with precise differential scanning calorimetry has revealed the MG state as an equilibrium intermediate state of the reversible thermal transition of the protein, and pressure perturbation calorimetry has succeeded in determining its volumetric properties. These examples strongly indicate the importance of a precise calorimetry and analysis model in the field of protein research.
ISSN:1557-7988
DOI:10.1016/bs.mie.2015.08.002