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...
Uloženo v:
| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1991
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| Témata: | |
| On-line přístup: | 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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