ArticleProceedings of the National Academy of Sciences of the United States of America2007
Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 40 citations in OpenAlex.
- Friends in need: How chaperonins recognize and remodel proteins that require folding assistance.Frontiers in molecular biosciences · 2022Review
- Integrated Computational Approaches and Tools forAllosteric Drug Discovery.International journal of molecular sciences · 2020Review
- Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.Nature chemical biology · 2018Article
- Coarse-Grained Simulations of Topology-Dependent Mechanisms of Protein Unfolding and Translocation Mediated by ClpY ATPase Nanomachines.PLoS computational biology · 2016Article
- Mechanism of substrate translocation by a ring-shaped ATPase motor at millisecond resolution.Journal of the American Chemical Society · 2015Article
- The allosteric communication pathways in KIX domain of CBP.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Chaperones: needed for both the good times and the bad times.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness.Molecular cell · 2013Article
- Computational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases.PLoS computational biology · 2011Article
- Assisted peptide folding by surface pattern recognition.Biophysical journal · 2011Article
- Unfolding and translocation pathway of substrate protein controlled by structure in repetitive allosteric cycles of the ClpY ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Article
- Reconciling theories of chaperonin accelerated folding with experimental evidence.Cellular and molecular life sciences : CMLS · 2010Review
- Perturbation-based Markovian transmission model for probing allosteric dynamics of large macromolecular assembling: a study of GroEL-GroES.PLoS computational biology · 2009Article
- CHARMM: the biomolecular simulation program.Journal of computational chemistry · 2009Review
- Kinetic model for the coupling between allosteric transitions in GroEL and substrate protein folding and aggregation.Journal of molecular biology · 2008Article
- GroEL stimulates protein folding through forced unfolding.Nature structural & molecular biology · 2008Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Escherichia coli chaperonin, GroEL, helps proteins fold under nonpermissive conditions. During the reaction cycle, GroEL undergoes allosteric transitions in response to binding of a substrate protein (SP), ATP, and the cochaperonin GroES. Using coarse-grained representations of the GroEL and GroES structures, we explore the link between allosteric transitions and the folding of a model SP, a de novo-designed four-helix bundle protein, with low spontaneous yield. The ensemble of GroEL-bound SP is less structured than the bulk misfolded structures. Upon binding, which kinetically occurs in two stages, the SP loses not only native tertiary contacts but also experiences a decrease in helical content. During multivalent binding and the subsequent ATP-driven transition of GroEL the SP undergoes force-induced stretching. Upon encapsulation, which occurs upon GroES binding, the SP finds itself in a "hydrophilic" cavity in which it can reach the folded conformation. Surprisingly, we find that the yield of the native state in the expanded GroEL cavity is relatively small even after it remains in it for twice the spontaneous folding time. Thus, in accord with the iterative annealing mechanism, multiple rounds of binding, partial unfolding, and release of the SP are required to enhance the yield of the folded SP.
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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.