title: Natural polypeptides in left-handed helical conformation. A circular dichroism study of the linker histones' C-terminal fragments and beta-endorphin.
abstract: Circular dichroism has been used to investigate the histone H1 and H5 C-terminal fragments and beta-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 degrees C. It was proposed to be due to non-cooperative disordering of the conformation caused by the destruction of the hydration shell.
authors.affiliation: Engelhardt Institute of Molecular Biology, Acad. Sci. Russia, Moscow.
authors.forename: A A
authors.initials: AA
authors.lastname: Makarov
authors.forename: V M
authors.initials: VM
authors.lastname: Lobachov
authors.forename: I A
authors.initials: IA
authors.lastname: Adzhubei
authors.forename: N G
authors.initials: NG
authors.lastname: Esipova
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D006657:Histones / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D013552:Swine; D013696:Temperature; D001615:beta-Endorphin / Q000737:chemistry*
chemical_list: D006657:Histones; D010455:Peptides; D001615:beta-Endorphin