Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding.

Circular dichroism and HPLC gel filtration were used to show that cytosolic hsp70 is thermally stable but undergoes a conformational transition (midpoint, 43 degrees C; 57 degrees C in the presence of ATP or ADP) leading to oligomerization. hsp70 binds to unfolded, but not to folded, proteins in a t...

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Detalles Bibliográficos

Publicado en:	Proc Natl Acad Sci U S A
Principais autores:	Palleros, D R, Welch, W J, Fink, A L
Formato:	Artigo
Idioma:	Inglês
Publicado:	National Academy of Sciences 1991
Assuntos:	Research Article
Acceso en liña:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC51949/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1829527/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.88.13.5719
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