From Conformation to Interaction: Techniques to Explore the Hsp70/Hsp90 Network.
Curr Protein Pept Sci
; 16(8): 735-53, 2015.
Article
em En
| MEDLINE
| ID: mdl-25961397
ABSTRACT
Proteins participate in almost every cell physiological function, and to do so, they need to reach a state that allows its function by folding and/or exposing surfaces of interactions. Spontaneous folding in the cell is in general hindered by its crowded and viscous environment, which favors misfolding and nonspecific and deleterious self-interactions. To overcome this, cells have a system, in which Hsp70 and Hsp90 play a central role to aid protein folding and avoid misfolding. The topics of this review include the biophysical tools used for monitoring protein-ligand and protein-protein interactions and also some important results related to the study of molecular chaperones and heat shock proteins (Hsp), with a focus on the Hsp70/Hsp90 network. The biophysical tools and their use to probe the conformation and interaction of Hsp70 and Hsp90 are briefly reviewed.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Choque Térmico HSP90
/
Proteínas de Choque Térmico HSP70
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article