Natural polypeptides in left-handed helical conformation. A circular dichroism study of the linker histones' C-terminal fragments and beta-endorphin.
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.
Makarov
A A
AA
Engelhardt Institute of Molecular Biology, Acad. Sci. Russia, Moscow.
Lobachov
V M
VM
Adzhubei
I A
IA
Esipova
N G
NG
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*
D006657:Histones; D010455:Peptides; D001615:beta-Endorphin