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Disulfide formation as a probe of folding in GroEL–GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones
The chaperonin GroEL assists protein folding by binding nonnative forms through exposed hydrophobic surfaces in an open ring and mediating productive folding in an encapsulated hydrophilic chamber formed when it binds GroES. Little is known about the topology of nonnative proteins during folding ins...
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| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
2007
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1793900/ https://ncbi.nlm.nih.gov/pubmed/17283341 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0610989104 |
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