ArticleJournal of molecular biology2008
Cotranslational folding promotes beta-helix formation and avoids aggregation in vivo.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- A detailed molecular picture of protein folding during active translation.bioRxiv : the preprint server for biology · 2026Article
- FoldDelay web server: an online tool to quantify translation-driven delays in protein native contact formation.Nucleic acids research · 2026Article
- Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026Article
- Native Fold Delay and its implications for co-translational chaperone binding and protein aggregation.Nature communications · 2025Article
- Article
- Translation Rates and Protein Folding.Journal of molecular biology · 2024Review
- AutoRNC: An automated modeling program for building atomic models of ribosome-nascent chain complexes.Structure (London, England : 1993) · 2024Article
- Mapping Protein-Protein Interactions at Birth: Single-Particle Cryo-EM Analysis of a Ribosome-Nascent Globin Complex.ACS central science · 2024Article
- How the ribosome shapes cotranslational protein folding.Current opinion in structural biology · 2024Review
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- A switch from α-helical to β-strand conformation during co-translational protein folding.The EMBO journal · 2022Article
- Peptides before and during the nucleotide world: an origins story emphasizing cooperation between proteins and nucleic acids.Journal of the Royal Society, Interface · 2022Review
- Slowest-first protein translation scheme: Structural asymmetry and co-translational folding.Biophysical journal · 2021Article
- Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein.Nature communications · 2021Article
- The Proteome Folding Problem and Cellular Proteostasis.Journal of molecular biology · 2021Review
- The Right-Handed Parallel β-Helix Topology ofBiomolecules · 2021Article
- Validation of DBFOLD: An efficient algorithm for computing folding pathways of complex proteins.PLoS computational biology · 2020Article
- Effect of Protein Structure on Evolution of Cotranslational Folding.Biophysical journal · 2020Article
- Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cotranslational Folding of Proteins on the Ribosome.Biomolecules · 2020Review
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Authors and funding
3 authors.
Funding
Abstract
Newly synthesized proteins must form their native structures in the crowded environment of the cell, while avoiding non-native conformations that can lead to aggregation. Yet, remarkably little is known about the progressive folding of polypeptide chains during chain synthesis by the ribosome or of the influence of this folding environment on productive folding in vivo. P22 tailspike is a homotrimeric protein that is prone to aggregation via misfolding of its central beta-helix domain in vitro. We have produced stalled ribosome:tailspike nascent chain complexes of four fixed lengths in vivo, in order to assess cotranslational folding of newly synthesized tailspike chains as a function of chain length. Partially synthesized, ribosome-bound nascent tailspike chains populate stable conformations with some native-state structural features even prior to the appearance of the entire beta-helix domain, regardless of the presence of the chaperone trigger factor, yet these conformations are distinct from the conformations of released, refolded tailspike truncations. These results suggest that organization of the aggregation-prone beta-helix domain occurs cotranslationally, prior to chain release, to a conformation that is distinct from the accessible energy minimum conformation for the truncated free chain in solution.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.