Nucleotide-Dependent Dimer Association and Dissociation of the Chaperone Hsp90.
J Phys Chem B
; 122(49): 11373-11380, 2018 12 13.
Article
en En
| MEDLINE
| ID: mdl-30179494
Hsp90 is an essential molecular chaperone, which has to be in a dimeric form for its correct function. While the affinity of the dimer has previously been measured, little is known about how it associates and dissociates and the factors that influence this. We perform an in-depth single molecule characterization of the C-terminal association and dissociation of Hsp90. We find more than one dissociation rate, indicating that the dimer has a stable and an unstable state. Furthermore, we find that the stability of the C-terminal association is dependent on the presence of ATP, despite the C-terminal dimerization interface being distal to the catalytic site.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas HSP90 de Choque Térmico
/
Nucleótidos
Tipo de estudio:
Risk_factors_studies
Idioma:
En
Revista:
J Phys Chem B
Asunto de la revista:
QUIMICA
Año:
2018
Tipo del documento:
Article
Pais de publicación:
Estados Unidos