ArticleProceedings of the National Academy of Sciences of the United States of America2018
Systematic mapping of free energy landscapes of a growing filamin domain during biosynthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 53 citations in OpenAlex.
- Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026Article
- Arrest Peptide Profiling resolves co-translational folding pathways and chaperone interactions in vivo.Nature communications · 2025Article
- Rational design ofNature communications · 2025Article
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Article
- The ribosome stabilizes partially folded intermediates of a nascent multi-domain protein.Nature chemistry · 2022Article
- Modulating co-translational protein folding by rational design and ribosome engineering.Nature communications · 2022Article
- Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022Review
- Cell-Free Synthesis Strategies to Probe Co-translational Folding of Proteins Within Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Common sequence motifs of nascent chains engage the ribosome surface and trigger factor.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Slowest-first protein translation scheme: Structural asymmetry and co-translational folding.Biophysical journal · 2021Article
- Interactions between nascent proteins and the ribosome surface inhibit co-translational folding.Nature chemistry · 2021Article
- An intrinsically disordered nascent protein interacts with specific regions of the ribosomal surface near the exit tunnel.Communications biology · 2021Article
- Nascent chain dynamics and ribosome interactions within folded ribosome-nascent chain complexes observed by NMR spectroscopy.Chemical science · 2021Article
- Co-translational folding of nascent polypeptides: Multi-layered mechanisms for the efficient biogenesis of functional proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021Article
- Optimal design of adaptively sampled NMR experiments for measurement of methyl group dynamics with application to a ribosome-nascent chain complex.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2021Article
- RepeatsDB in 2021: improved data and extended classification for protein tandem repeat structures.Nucleic acids research · 2021Article
- Analysis of conformational exchange processes using methyl-TROSY-based Hahn echo measurements of quadruple-quantum relaxation.Magnetic resonance (Gottingen, Germany) · 2021Article
- Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Gradual compaction of the nascent peptide during cotranslational folding on the ribosome.eLife · 2020Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Cotranslational folding (CTF) is a fundamental molecular process that ensures efficient protein biosynthesis and minimizes the formation of misfolded states. However, the complexity of this process makes it extremely challenging to obtain structural characterizations of CTF pathways. Here, we correlate observations of translationally arrested nascent chains with those of a systematic C-terminal truncation strategy. We create a detailed description of chain length-dependent free energy landscapes associated with folding of the FLN5 filamin domain, in isolation and on the ribosome, and thus, quantify a substantial destabilization of the native structure on the ribosome. We identify and characterize two folding intermediates formed in isolation, including a partially folded intermediate associated with the isomerization of a conserved cis proline residue. The slow folding associated with this process raises the prospect that neighboring unfolded domains might accumulate and misfold during biosynthesis. We develop a simple model to quantify the risk of misfolding in this situation and show that catalysis of folding by peptidyl-prolyl isomerases is sufficient to eliminate this hazard.
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