A thermodynamic coupling mechanism for GroEL-mediated unfolding.
Chaperonins prevent the aggregation of partially folded or misfolded forms of a protein and, thus, keep it competent for productive folding. It was suggested that GroEL, the chaperonin of Escherichia coli, exerts this function 1 unfolding such intermediates, presumably in a catalytic fashion. We inv...
Uloženo v:
| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1996
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC38444/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8790346/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.93.18.9425 |
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