Intermediate States of Apomyoglobin: Are They Parts of the Same Area of Conformations Diagram?

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V. A. Balobanov^*, N. S. Katina, A. V. Finkelstein, and V. E. Bychkova

Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: uralm62@rambler.ru

^* To whom correspondence should be addressed.

Received September 23, 2016; Revision received December 30, 2016

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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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KEY WORDS: apomyoglobin, conformational transitions, conformations diagram, intermediate state

DOI: 10.1134/S0006297917050108

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