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Natural polypeptides in left‐handed helical conformation A circular dichroism study of the linker histones’ C‐terminal fragments and β‐endorphin
Author(s) -
Makarov A.A.,
Lobachov V.M.,
Adzhubei I.A.,
Esipova N.G.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80838-8
Subject(s) - circular dichroism , chemistry , crystallography , linker , left handed , stereochemistry , physics , optics , computer science , operating system
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.