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Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90
The heat shock protein 90 (Hsp90) is a molecular chaperone that employs the free energy of ATP hydrolysis to control the folding and activation of several client proteins in the eukaryotic cell. To elucidate how the local ATPase reaction in the active site couples to the global conformational dynami...
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| 出版年: | Nat Commun |
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| 主要な著者: | , , , , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Nature Publishing Group UK
2020
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7075974/ https://ncbi.nlm.nih.gov/pubmed/32179743 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-020-15050-0 |
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