ArticleNature protocols2016
A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.
Article in Nature protocols, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 55 citations in OpenAlex.
- 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
- Hydrogen/deuterium exchange mass spectrometry analysis of ribosome-nascent chain complexes to study protein biogenesis at the peptide level.Nature protocols · 2026Article
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking.Nature structural & molecular biology · 2025Article
- Rational design ofNature communications · 2025Article
- Resolving chaperone-assisted protein folding on the ribosome at the peptide level.Nature structural & molecular biology · 2024Article
- HCP5 Derived Novel Microprotein Triggers Progression of Gastric Cancer through Regulating Ferroptosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Article
- Thermodynamic profiles for cotranslational trigger factor substrate recognition.Science advances · 2024Article
- Insights into the ribosome function from the structures of non-arrested ribosome-nascent chain complexes.Nature chemistry · 2023Article
- The ribosome stabilizes partially folded intermediates of a nascent multi-domain protein.Nature chemistry · 2022Article
- Multi-layer sequential network analysis improves protein 3D structural classification.Proteins · 2022Article
- Modulating co-translational protein folding by rational design and ribosome engineering.Nature communications · 2022Article
- Cell-Free Synthesis Strategies to Probe Co-translational Folding of Proteins Within Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022Review
- 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
- Interactions between nascent proteins and the ribosome surface inhibit co-translational folding.Nature chemistry · 2021Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
During biosynthesis on the ribosome, an elongating nascent polypeptide chain can begin to fold, in a process that is central to all living systems. Detailed structural studies of co-translational protein folding are now beginning to emerge; such studies were previously limited, at least in part, by the inherently dynamic nature of emerging nascent chains, which precluded most structural techniques. NMR spectroscopy is able to provide atomic-resolution information for ribosome-nascent chain complexes (RNCs), but it requires large quantities (≥10 mg) of homogeneous, isotopically labeled RNCs. Further challenges include limited sample working concentration and stability of the RNC sample (which contribute to weak NMR signals) and resonance broadening caused by attachment to the large (2.4-MDa) ribosomal complex. Here, we present a strategy to generate isotopically labeled RNCs in Escherichia coli that are suitable for NMR studies. Uniform translational arrest of the nascent chains is achieved using a stalling motif, and isotopically labeled RNCs are produced at high yield using high-cell-density E. coli growth conditions. Homogeneous RNCs are isolated by combining metal affinity chromatography (to isolate ribosome-bound species) with sucrose density centrifugation (to recover intact 70S monosomes). Sensitivity-optimized NMR spectroscopy is then applied to the RNCs, combined with a suite of parallel NMR and biochemical analyses to cross-validate their integrity, including RNC-optimized NMR diffusion measurements to report on ribosome attachment in situ. Comparative NMR studies of RNCs with the analogous isolated proteins permit a high-resolution description of the structure and dynamics of a nascent chain during its progressive biosynthesis on the ribosome.
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