Scanning microcalorimetry and circular dichroism study of melting of the natural polypeptides in the left-handed helical conformation.
J Protein Chem
; 12(1): 85-91, 1993 Feb.
Article
en En
| MEDLINE
| ID: mdl-8381285
ABSTRACT
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Conformación Proteica
/
Desnaturalización Proteica
/
Betaendorfina
/
Hormona Adrenocorticotrópica
Límite:
Animals
Idioma:
En
Revista:
J Protein Chem
Año:
1993
Tipo del documento:
Article