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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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| Format: | Artikel |
| Sprache: | en |
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1991
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| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC51949/ https://ncbi.nlm.nih.gov/pubmed/1829527 |
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