Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram?
- Авторы: Balobanov V.1, Katina N.1, Finkelstein A.1, Bychkova V.1
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Учреждения:
- Institute of Protein Research
- Выпуск: Том 82, № 5 (2017)
- Страницы: 625-631
- Раздел: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/151388
- DOI: https://doi.org/10.1134/S0006297917050108
- ID: 151388
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Аннотация
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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Об авторах
V. Balobanov
Institute of Protein Research
Автор, ответственный за переписку.
Email: uralm62@rambler.ru
Россия, Pushchino, Moscow Region, 142290
N. Katina
Institute of Protein Research
Email: uralm62@rambler.ru
Россия, Pushchino, Moscow Region, 142290
A. Finkelstein
Institute of Protein Research
Email: uralm62@rambler.ru
Россия, Pushchino, Moscow Region, 142290
V. Bychkova
Institute of Protein Research
Email: uralm62@rambler.ru
Россия, Pushchino, Moscow Region, 142290
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