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The driving force for co-translational protein folding is weaker in the ribosome vestibule due to greater water ordering
Interactions between the ribosome and nascent chain can destabilize folded domains in the ribosome exit tunnel's vestibule, the last 3 nm of the exit tunnel where tertiary folding can occur. Here, we test if a contribution to this destabilization is a weakening of hydrophobic association, the d...
| Autores principales: | , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
The Royal Society of Chemistry
2021
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8442680/ https://www.ncbi.nlm.nih.gov/pubmed/34659725 http://dx.doi.org/10.1039/d1sc01008e |