ArticleNature communications2019
Non-equilibrium dynamics of a nascent polypeptide during translation suppress its misfolding.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Quasi-continuous cotranslational compaction and folding of a multidomain protein.Nature communications · 2026Article
- A detailed molecular picture of protein folding during active translation.bioRxiv : the preprint server for biology · 2026Article
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026Article
- Bacterial chromosome conformation and cell-free gene expression in synthetic 2D compartments.Nature communications · 2025Article
- How Sup35 monomer conformation and amyloid fibril polymorphism determine yeast strain phenotypes.Research square · 2025Article
- DNA origami-enhanced force spectroscopy and AlphaFold structural analyses reveal the folding landscape of calcium-binding proteins.Science advances · 2025Article
- Translation Rates and Protein Folding.Journal of molecular biology · 2024Review
- Thermodynamic profiles for cotranslational trigger factor substrate recognition.Science advances · 2024Article
- AutoRNC: An automated modeling program for building atomic models of ribosome-nascent chain complexes.Structure (London, England : 1993) · 2024Article
- A genetic circuit on a single DNA molecule as an autonomous dissipative nanodevice.Nature communications · 2024Article
- RNA-seq reveals multifaceted gene expression response to Fab production in Escherichia coli fed-batch processes with particular focus on ribosome stalling.Microbial cell factories · 2024Article
- Investigation of metal ion binding biomolecules one molecule at a time.Frontiers in chemistry · 2024Review
- Folding correctors can restore CFTR posttranslational folding landscape by allosteric domain-domain coupling.Nature communications · 2023Article
- Co-translational formation of disulfides guides folding of the SARS-CoV-2 receptor binding domain.Biophysical journal · 2023Article
- Is Posttranslational Folding More Efficient Than Refolding from a Denatured State: A Computational Study.The journal of physical chemistry. B · 2023Article
- Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?International journal of molecular sciences · 2022Review
- Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022Review
- Interactions between nascent proteins and the ribosome surface inhibit co-translational folding.Nature chemistry · 2021Article
- Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein.Nature communications · 2021Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Protein folding can begin co-translationally. Due to the difference in timescale between folding and synthesis, co-translational folding is thought to occur at equilibrium for fast-folding domains. In this scenario, the folding kinetics of stalled ribosome-bound nascent chains should match the folding of nascent chains in real time. To test if this assumption is true, we compare the folding of a ribosome-bound, multi-domain calcium-binding protein stalled at different points in translation with the nascent chain as is it being synthesized in real-time, via optical tweezers. On stalled ribosomes, a misfolded state forms rapidly (1.5 s). However, during translation, this state is only attained after a long delay (63 s), indicating that, unexpectedly, the growing polypeptide is not equilibrated with its ensemble of accessible conformations. Slow equilibration on the ribosome can delay premature folding until adequate sequence is available and/or allow time for chaperone binding, thus promoting productive folding.
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