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Conformational dynamics of bacterial trigger factor in apo and ribosome-bound states
The chaperone trigger factor (TF) binds to the ribosome exit tunnel and helps cotranslational folding of nascent chains (NC) in bacterial cells and chloroplasts. In this study, we aim to investigate the functional dynamics of fully-atomistic apo TF and its complex with 50S. As TF accomodates a high...
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| Pubblicato in: | PLoS One |
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| Autori principali: | , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Public Library of Science
2017
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5402958/ https://ncbi.nlm.nih.gov/pubmed/28437479 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0176262 |
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