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

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Abstract

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.

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Abbreviations

ApoMb:

apomyoglobin

CD:

circular dichroism

DSC:

differential scanning calorimetry

I:

protein intermediate state

N:

protein native state

U:

protein unfolded state

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Authors and Affiliations

  1. Institute of Protein Research, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia

    V. A. Balobanov, N. S. Katina, A. V. Finkelstein & V. E. Bychkova

Authors
  1. V. A. Balobanov
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  2. N. S. Katina
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  3. A. V. Finkelstein
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  4. V. E. Bychkova
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Correspondence to V. A. Balobanov.

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Published in Russian in Biokhimiya, 2017, Vol. 82, No. 5, pp. 832-840.

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Balobanov, V.A., Katina, N.S., Finkelstein, A.V. et al. Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram?. Biochemistry Moscow 82, 625–631 (2017). https://doi.org/10.1134/S0006297917050108

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  • DOI: https://doi.org/10.1134/S0006297917050108

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