Scanning microcalorimetry and circular dichroism study of melting of the natural polypeptides in the left-handed helical conformation.
It has been shown that in aqueous solution histone H1 and H5 C-terminal fragments and peptide hormones beta-endorphin and ACTH adopt preferably the left-handed helical conformation of the poly-L-proline II type. Scanning microcalorimetry and circular dichroism have been used to show that the linear temperature dependence of CD maximum amplitude and partial heat capacity value are broken in the temperature interval between 50 and 60 degrees C, after which [C]p reaches the constant level. It was proposed to be due to noncooperative disordering of the conformation caused by the destruction of the polypeptide hydration shell.
Engelhardt Institute of Molecular Biology, Acad. Sci. Russia, Moscow.
A A
AA
Makarov
I A
IA
Adzhubei
I I
II
Protasevich
V M
VM
Lobachov
N G
NG
Esipova
D000324:Adrenocorticotropic Hormone / Q000737:chemistry*; D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D002645:Chickens; D002942:Circular Dichroism; D006358:Hot Temperature; D010455:Peptides / Q000737:chemistry; D010903:Pituitary Gland, Anterior / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D013552:Swine; D001615:beta-Endorphin / Q000737:chemistry*
D010455:Peptides; C011083:polyproline; D001615:beta-Endorphin; D000324:Adrenocorticotropic Hormone