Ornithine carbamoyltransferase unfolding states in the presence of urea and guanidine hydrochloride.
Appl Biochem Biotechnol
; 172(2): 854-66, 2014 Jan.
Article
en En
| MEDLINE
| ID: mdl-24122710
Ornithine carbamoyltransferase folding/unfolding is a complex and not completely understood process. Our experimental results suggest that ornithine carbamoyltransferase interacts in a completely different way with urea and guanidine hydrochloride. In fact, we noticed that, increasing concentration from 0.0 to 8.0 M of the two additives, the enzyme follows a simple one-step transition mechanism in the presence of guanidine hydrochloride, with two macroscopic states (the native and the denatured one) significantly populated, whereas in the presence of urea a lot of different protein states can be detected and analyzed. Circular dichroism and UV-visible spectroscopy reveal a similar mechanism of perturbation at high temperature, with opening of hydrophobic core and a significant loss in α-helix structure in the presence of guanidine hydrochloride that cannot be found in the presence of urea.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ornitina Carbamoiltransferasa
/
Urea
/
Pliegue de Proteína
/
Guanidina
Límite:
Animals
Idioma:
En
Revista:
Appl Biochem Biotechnol
Año:
2014
Tipo del documento:
Article
Pais de publicación:
Estados Unidos