ArticleJournal of molecular biology2006
Effect of hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chain.
Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- 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
- Distribution and solvent exposure of Hsp70 chaperone binding sites across the Escherichia coli proteome.Proteins · 2023Article
- Review
- Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.The Biochemical journal · 2019Review
- Article
- Competing Pathways and Multiple Folding Nuclei in a Large Multidomain Protein, Luciferase.Biophysical journal · 2017Article
- Hsp70 biases the folding pathways of client proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A novel tri-enzyme system in combination with laser-driven NMR enables efficient nuclear polarization of biomolecules in solution.The journal of physical chemistry. B · 2013Article
- Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system.Protein science : a publication of the Protein Society · 2012Article
- Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery.Protein science : a publication of the Protein Society · 2012Article
- 1H-Detected 13C photo-CIDNP as a sensitivity enhancement tool in solution NMR.Journal of the American Chemical Society · 2011Article
- Conformational dynamics of the molecular chaperone Hsp90.Quarterly reviews of biophysics · 2011Review
- High-resolution conformation and backbone dynamics of a soluble aggregate of apomyoglobin119.Biophysical journal · 2011Article
- Contribution of long-range interactions to the secondary structure of an unfolded globin.Biophysical journal · 2010Article
- Confined dynamics of a ribosome-bound nascent globin: Cone angle analysis of fluorescence depolarization decays in the presence of two local motions.Protein science : a publication of the Protein Society · 2009Article
- Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide.Protein science : a publication of the Protein Society · 2009Article
- pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation.Journal of molecular biology · 2009Article
- Nonnative helical motif in a chaperone-bound protein fragment.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Virtually nothing is known about the interaction of co-translationally active chaperones with nascent polypeptides and the resulting effects on peptide conformation and folding. We have explored this issue by NMR analysis of apomyoglobin N-terminal fragments of increasing length, taken as models for different stages of protein biosynthesis, in the absence and presence of the substrate binding domain of Escherichia coli Hsp70, DnaK-beta. The incomplete polypeptides misfold and self-associate under refolding conditions. In the presence of DnaK-beta, however, formation of the original self-associated species is completely or partially prevented. Chaperone interaction with incomplete protein chains promotes a globally unfolded dynamic DnaK-beta-bound state, which becomes folding-competent only upon incorporation of the residues corresponding to the C-terminal H helix. The chaperone does not bind the full-length protein at equilibrium. However, its presence strongly disfavors the kinetic accessibility of misfolding side-routes available to the full-length chain. This work supports the role of DnaK as a "holder" for incomplete N-terminal polypeptides. However, as the chain approaches its full-length status, the tendency to intramolecularly bury non-polar surface efficiently outcompetes chaperone binding. Under these conditions, DnaK serves as a "folding enhancer" by supporting folding of a population of otherwise folding-incompetent full-length protein chains.
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Registered trials
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.