ArticleBiophysical journal2016
Conformations of a Metastable SH3 Domain Characterized by smFRET and an Excluded-Volume Polymer Model.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Learning to evolve structural ensembles of unfolded and disordered proteins using experimental solution data.The Journal of chemical physics · 2023Article
- Distribution and solvent exposure of Hsp70 chaperone binding sites across the Escherichia coli proteome.Proteins · 2023Article
- IDPConformerGenerator: A Flexible Software Suite for Sampling the Conformational Space of Disordered Protein States.The journal of physical chemistry. A · 2022Article
- Protein Dynamics to Define and Refine Disordered Protein Ensembles.The journal of physical chemistry. B · 2022Article
- Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins.Methods (San Diego, Calif.) · 2021Article
- Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Extraction of rapid kinetics from smFRET measurements using integrative detectors.Cell reports. Physical science · 2021Article
- Generalizing HMMs to Continuous Time for Fast Kinetics: Hidden Markov Jump Processes.Biophysical journal · 2021Article
- Non-cooperative 4E-BP2 folding with exchange between eIF4E-binding and binding-incompatible states tunes cap-dependent translation inhibition.Nature communications · 2020Article
- Submillisecond Freezing Permits Cryoprotectant-Free EPR Double Electron-Electron Resonance Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- Assessing Site-Specific Enhancements Imparted by Hyperpolarized Water in Folded and Unfolded Proteins by 2D HMQC NMR.Journal of the American Chemical Society · 2020Article
- Extended Experimental Inferential Structure Determination Method in Determining the Structural Ensembles of Disordered Protein States.Communications chemistry · 2020Article
- Structural metamorphism and polymorphism in proteins on the brink of thermodynamic stability.Protein science : a publication of the Protein Society · 2018Review
- Conformational Heterogeneity and FRET Data Interpretation for Dimensions of Unfolded Proteins.Biophysical journal · 2017Article
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9 authors.
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Abstract
Conformational states of the metastable drkN SH3 domain were characterized using single-molecule fluorescence techniques. Under nondenaturing conditions, two Förster resonance energy transfer (FRET) populations were observed that corresponded to a folded and an unfolded state. FRET-estimated radii of gyration and hydrodynamic radii estimated by fluorescence correlation spectroscopy of the two coexisting conformations are in agreement with previous ensemble x-ray scattering and NMR measurements. Surprisingly, when exposed to high concentrations of urea and GdmCl denaturants, the protein still exhibits two distinct FRET populations. The dominant conformation is expanded, showing a low FRET efficiency, consistent with the expected behavior of a random chain with excluded volume. However, approximately one-third of the drkN SH3 conformations showed high, nearly 100%, FRET efficiency, which is shown to correspond to denaturation-induced looped conformations that remain stable on a timescale of at least 100 μs. These loops may contain interconverting conformations that are more globally collapsed, hairpin-like, or circular, giving rise to the observed heterogeneous broadening of this population. Although the underlying mechanism of chain looping remains elusive, FRET experiments in formamide and dimethyl sulfoxide suggest that interactions between hydrophobic groups in the distal regions may play a significant role in the formation of the looped state.
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