Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
The chaperonin GroEL binds nonnative proteins in its central channel through hydrophobic interactions and initiates productive folding in this space underneath bound cochaperone, GroES, in the presence of ATP. The questions of where along the folding pathway a protein is recognized by GroEL, and how...
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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1997
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC19747/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9037009/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.94.4.1080 |
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