Natural polypeptides in left‐handed helical conformation A circular dichroism study of the linker histones’ C‐terminal fragments and β‐endorphin

FEBS Letters

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