Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.
Free GroEL binds denatured proteins very tightly: it retards the folding of barnase 400-fold and catalyzes unfolding fluctuations in native barnase and its folding intermediate. GroEL undergoes an allosteric transition from its tight-binding T-state to a weaker binding R-state on the cooperative bin...
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| Udgivet i: | Proc Natl Acad Sci U S A |
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| Principais autores: | , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
National Academy of Sciences
1996
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC39569/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8633099/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.93.9.4509 |
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