Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram?
- 作者: Balobanov V.1, Katina N.1, Finkelstein A.1, Bychkova V.1
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隶属关系:
- Institute of Protein Research
- 期: 卷 82, 编号 5 (2017)
- 页面: 625-631
- 栏目: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/151388
- DOI: https://doi.org/10.1134/S0006297917050108
- ID: 151388
如何引用文章
详细
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.
作者简介
V. Balobanov
Institute of Protein Research
编辑信件的主要联系方式.
Email: uralm62@rambler.ru
俄罗斯联邦, Pushchino, Moscow Region, 142290
N. Katina
Institute of Protein Research
Email: uralm62@rambler.ru
俄罗斯联邦, Pushchino, Moscow Region, 142290
A. Finkelstein
Institute of Protein Research
Email: uralm62@rambler.ru
俄罗斯联邦, Pushchino, Moscow Region, 142290
V. Bychkova
Institute of Protein Research
Email: uralm62@rambler.ru
俄罗斯联邦, Pushchino, Moscow Region, 142290
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