ArticleProtein science : a publication of the Protein Society2009
Confined dynamics of a ribosome-bound nascent globin: Cone angle analysis of fluorescence depolarization decays in the presence of two local motions.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- Nascent chains derived from a foldable protein sequence interact with specific ribosomal surface sites near the exit tunnel.Scientific reports · 2024Article
- Mapping Protein-Protein Interactions at Birth: Single-Particle Cryo-EM Analysis of a Ribosome-Nascent Globin Complex.ACS central science · 2024Article
- Critical Beginnings: Selective Tuning of Solubility and Structural Accuracy of Newly Synthesized Proteins by the Hsp70 Chaperone System.The journal of physical chemistry. B · 2023Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- An intrinsically disordered nascent protein interacts with specific regions of the ribosomal surface near the exit tunnel.Communications biology · 2021Article
- Fluorescence Anisotropy Decays and Microscale-Volume Viscometry Reveal the Compaction of Ribosome-Bound Nascent Proteins.The journal of physical chemistry. B · 2021Article
- Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Time-resolved multirotational dynamics of single solution-phase tau proteins reveals details of conformational variation.Physical chemistry chemical physics : PCCP · 2019Article
- Folding up and Moving on-Nascent Protein Folding on the Ribosome.Journal of molecular biology · 2018Review
- Unraveling co-translational protein folding: Concepts and methods.Methods (San Diego, Calif.) · 2018Review
- Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level.Angewandte Chemie (International ed. in English) · 2017Article
- The Ribosome Restrains Molten Globule Formation in Stalled Nascent Flavodoxin.The Journal of biological chemistry · 2016Article
- Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Nonorthogonal tRNA(cys)(Amber) for protein and nascent chain labeling.RNA (New York, N.Y.) · 2015Article
- Protein folding on the ribosome studied using NMR spectroscopy.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- Autotransporters: The Cellular Environment Reshapes a Folding Mechanism to Promote Protein Transport.The journal of physical chemistry letters · 2012Article
- Crowding effects on the small, fast-folding protein lambda6-85.Faraday discussions · 2012Article
- Protein folding at the exit tunnel.Annual review of biophysics · 2011Review
- Dynamic fluorescence depolarization: a powerful tool to explore protein folding on the ribosome.Methods (San Diego, Calif.) · 2010Review
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We still know very little about how proteins achieve their native three-dimensional structure in vitro and in the cell. Folding studies as proteins emerge from the mega Dalton-sized ribosome pose special challenges due to the large size and complicated nature of the ribosome-nascent chain complex. This work introduces a combination of three-component analysis of fluorescence depolarization decays (including the presence of two local motions) and in-cone analysis of diffusive local dynamics to investigate the spatial constraints experienced by a protein emerging from the ribosomal tunnel. We focus on E. coli ribosomes and an all-alpha-helical nascent globin in the presence and absence of the cotranslationally active chaperones DnaK and trigger factor. The data provide insights on the dynamic nature and structural plasticity of ribosome-nascent chain complexes. We find that the sub-ns motions of the N-terminal fluorophore, reporting on the globin dynamics in the vicinity of the N terminus, are highly constrained both inside and outside the ribosomal tunnel, resulting in high-order parameters (>0.85) and small cone semiangles (<30 degrees ). The shorter globin chains buried inside the tunnel are less spatially constrained than those of a reference sequence from a natively unfolded protein, suggesting either that the two nascent chain sequences have a different secondary structure and therefore sample different regions of the tunnel or that the tunnel undergoes local structural adjustments to accommodate the globin sequence. Longer globins emerging out of the ribosomal tunnel are also found to have highly spatially constrained slow (ns) motions. There are no observable spectroscopic changes in the absence of bound chaperones.
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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.