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

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

DOI: 10.1134/S0006297917050108