ArticleProceedings of the National Academy of Sciences of the United States of America2009
Direct single-molecule observation of a protein living in two opposed native structures.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 78 citations in OpenAlex.
- The Curious Case of A31P, a Topology-Switching Mutant of the Repressor of Primer Protein: A Molecular Dynamics Study of Its Folding and Misfolding.Journal of chemical information and modeling · 2024Article
- Metamorphic proteins and how to find them.Current opinion in structural biology · 2024Review
- Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins.Biomolecules · 2021Review
- Computational design of closely related proteins that adopt two well-defined but structurally divergent folds.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Single-molecule detection on a portable 3D-printed microscope.Nature communications · 2019Article
- Sliding Mechanism at a Coiled-Coil Interface.Biophysical journal · 2019Article
- Homodimerization regulates an endothelial specific signature of the SOX18 transcription factor.Nucleic acids research · 2018Article
- Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Munc18-1 is a molecular chaperone for α-synuclein, controlling its self-replicating aggregation.The Journal of cell biology · 2016Article
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- Confocal Spectroscopy to Study Dimerization, Oligomerization and Aggregation of Proteins: A Practical Guide.International journal of molecular sciences · 2016Review
- Conformations of a Metastable SH3 Domain Characterized by smFRET and an Excluded-Volume Polymer Model.Biophysical journal · 2016Article
- Review
- Protein stability: computation, sequence statistics, and new experimental methods.Current opinion in structural biology · 2015Review
- Interdomain Contacts Control Native State Switching of RfaH on a Dual-Funneled Landscape.PLoS computational biology · 2015Article
- Forced folding of a disordered protein accesses an alternative folding landscape.Chemphyschem : a European journal of chemical physics and physical chemistry · 2015Article
- Frustration in biomolecules.Quarterly reviews of biophysics · 2014Review
- Rapid mapping of interactions between Human SNX-BAR proteins measured in vitro by AlphaScreen and single-molecule spectroscopy.Molecular & cellular proteomics : MCP · 2014Article
- Structural plasticity of 4-α-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Cortactin scaffolds Arp2/3 and WAVE2 at the epithelial zonula adherens.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Biological activity in proteins requires them to share the energy landscape for folding and global conformational motions, 2 key determinants of function. Although most structural studies to date have focused on fluctuations around a single structural basin, we directly observe the coexistence of 2 symmetrically opposed conformations for a mutant of the Rop-homodimer (Repressor of Primer) in single-molecule fluorescence resonance energy transfer (smFRET) measurements. We find that mild denaturing conditions can affect the sensitive balance between the conformations, generating an equilibrium ensemble consisting of 2 equally occupied structural basins. Despite the need for large-scale conformational rearrangement, both native structures are dynamically and reversibly adopted for the same paired molecules without separation of the constituent monomers. Such an ability of some proteins or protein complexes to switch between conformations by thermal fluctuations and/or minor environmental changes could be central to their ability to control biological function.
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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.