Natural polypeptides in left‐handed helical conformation A circular dichroism study of the linker histones’ C‐terminal fragments and β‐endorphin
- 13 July 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 306 (1) , 63-65
- https://doi.org/10.1016/0014-5793(92)80838-8
Abstract
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.Keywords
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