期刊论文详细信息
FEBS Letters | |
Natural polypeptides in left‐handed helical conformation A circular dichroism study of the linker histones’ C‐terminal fragments and β‐endorphin | |
Makarov, A.A.1  Adzhubei, I.A.2  Esipova, N.G.1  Lobachov, V.M.1  | |
[1] Engelhardt Institute of Molecular Biology, Acad. Sci. Russia, Vavilova Str. 32, Moscow 117984, Russia;Department of Molecular Biology, Faculty of Biology, Lomonosov, Moscow State University, Moscow 119899, Russia | |
关键词: Linker histone; β-Endorphin; Circular dichroism; Poly-l-proline II conformation; Non-cooperative melting; | |
DOI : 10.1016/0014-5793(92)80838-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Circular dichroism has been used to investigate the histone HI and H5 C-terminal fragments and β-endorphin conformation. It has been shown that in aqueous solution these polypeptides preferably adopt the left-handed helical conformation of the poly-l-proline II type. A break in the linear temperature dependence of the CD value was found in the temperature interval between 50 and 55°C. It was proposed to be due to non-cooperative disordering of the conformation caused by the destruction of the hydration shell.
【 授权许可】
Unknown
【 预 览 】
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