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Updated: Feb 28, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
Intermediate States of Apomyoglobin: Are They Parts of the Same Area of Conformations Diagram?
V A Balobanov1, N S Katina, A V Finkelstein
1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. uralm62@rambler.ru.
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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