Biochemistry (Moscow)

, Volume 82, Issue 5, pp 625–631 | Cite as

Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram?

  • V. A. BalobanovEmail author
  • N. S. Katina
  • A. V. Finkelstein
  • V. E. Bychkova


Several research teams have reported detection and characterization of various apomyoglobin intermediate states different in their accumulation mode, thus putting a natural question as to proportions of these intermediates. The current report presents spectral properties of sperm whale apomyoglobin studied over a wide range of conditions with the use of circular dichroism and fluorescence techniques. Based on the experimental data, a diagram of apomyoglobin conformational states has been constructed. It shows that though induced by various denaturants, all the observed intermediates belong to one and the same area in the diagram.


apomyoglobin conformational transitions conformations diagram intermediate state 





circular dichroism


differential scanning calorimetry


protein intermediate state


protein native state


protein unfolded state


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Copyright information

© Pleiades Publishing, Ltd. 2017

Authors and Affiliations

  • V. A. Balobanov
    • 1
    Email author
  • N. S. Katina
    • 1
  • A. V. Finkelstein
    • 1
  • V. E. Bychkova
    • 1
  1. 1.Institute of Protein ResearchRussian Academy of SciencesPushchino, Moscow RegionRussia

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