ReviewProgress in nuclear magnetic resonance spectroscopy2013
Protein folding on the ribosome studied using NMR spectroscopy.
Review in Progress in nuclear magnetic resonance spectroscopy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 41 citations in OpenAlex.
- EPR spectroscopy in the study of ribosomal complexes.Biophysical reviews · 2025Review
- Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-TerminalMolecules (Basel, Switzerland) · 2023Article
- Polymer Dynamics in Glycerol-Water Mixtures.Molecules (Basel, Switzerland) · 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
- 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
- Capturing Membrane Protein Ribosome Nascent Chain Complexes in a Native-like Environment for Co-translational Studies.Biochemistry · 2020Article
- Unraveling co-translational protein folding: Concepts and methods.Methods (San Diego, Calif.) · 2018Review
- Article
- A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.Nature protocols · 2016Article
- Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations.Molecular cell · 2016Article
- Article
- Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.Journal of biomolecular NMR · 2015Article
- Cotranslational Protein Folding inside the Ribosome Exit Tunnel.Cell reports · 2015Article
- KnotProt: a database of proteins with knots and slipknots.Nucleic acids research · 2015Article
- The amyloid state and its association with protein misfolding diseases.Nature reviews. Molecular cell biology · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
NMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding, providing a characterization of molecular structure, dynamics and exchange processes, across a very wide range of timescales and with near atomic resolution. In recent years NMR methods have also been developed to study protein folding as it might occur within the cell, in a de novo manner, by observing the folding of nascent polypeptides in the process of emerging from the ribosome during synthesis. Despite the 2.3 MDa molecular weight of the bacterial 70S ribosome, many nascent polypeptides, and some ribosomal proteins, have sufficient local flexibility that sharp resonances may be observed in solution-state NMR spectra. In providing information on dynamic regions of the structure, NMR spectroscopy is therefore highly complementary to alternative methods such as X-ray crystallography and cryo-electron microscopy, which have successfully characterized the rigid core of the ribosome particle. However, the low working concentrations and limited sample stability associated with ribosome-nascent chain complexes means that such studies still present significant technical challenges to the NMR spectroscopist. This review will discuss the progress that has been made in this area, surveying all NMR studies that have been published to date, and with a particular focus on strategies for improving experimental sensitivity.
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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.