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Importance of cycle timing for the function of the molecular chaperone Hsp90
Hsp90 couples ATP hydrolysis to large conformational changes essential for activation of client proteins. The structural transitions involve dimerization of the N-terminal domains and formation of ‘closed states’ involving the N-terminal and middle domains. Here, we used Hsp90 mutants that modulate...
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| Gepubliceerd in: | Nat Struct Mol Biol |
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| Hoofdauteurs: | , , , , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
2016
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6248305/ https://ncbi.nlm.nih.gov/pubmed/27723736 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/nsmb.3305 |
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