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Mapping the conformation of a client protein through the Hsp70 functional cycle
The 70 kDa heat shock protein (Hsp70) chaperone system is ubiquitous, highly conserved, and involved in a myriad of diverse cellular processes. Its function relies on nucleotide-dependent interactions with client proteins, yet the structural features of folding-competent substrates in their Hsp70-bo...
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| Gepubliceerd in: | Proc Natl Acad Sci U S A |
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| Hoofdauteurs: | , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
National Academy of Sciences
2015
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4547247/ https://ncbi.nlm.nih.gov/pubmed/26240333 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1508504112 |
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