ArticleBiophysical journal2017
Conformational Heterogeneity and FRET Data Interpretation for Dimensions of Unfolded Proteins.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- From possibility to precision in macromolecular ensemble prediction.Nature methods · 2026Article
- Intrinsic stiffness andPNAS nexus · 2025Article
- A genetically encoded anomalous SAXS ruler to probe the dimensions of intrinsically disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Intrinsically disordered regions are poised to act as sensors of cellular chemistry.Trends in biochemical sciences · 2023Review
- SOURSOP: A Python Package for the Analysis of Simulations of Intrinsically Disordered Proteins.Journal of chemical theory and computation · 2023Article
- Intramolecular structural heterogeneity altered by long-range contacts in an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- The Analytical Flory Random Coil Is a Simple-to-Use Reference Model for Unfolded and Disordered Proteins.The journal of physical chemistry. B · 2023Article
- The analytical Flory random coil is a simple-to-use reference model for unfolded and disordered proteins.bioRxiv : the preprint server for biology · 2023Article
- Article
- Unraveling multi-state molecular dynamics in single-molecule FRET experiments. I. Theory of FRET-lines.The Journal of chemical physics · 2022Article
- Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins.Methods (San Diego, Calif.) · 2021Article
- Conformational Ensembles of an Intrinsically Disordered Protein Consistent with NMR, SAXS, and Single-Molecule FRET.Journal of the American Chemical Society · 2020Article
- Hydropathy Patterning Complements Charge Patterning to Describe Conformational Preferences of Disordered Proteins.The journal of physical chemistry letters · 2020Article
- Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Extended Experimental Inferential Structure Determination Method in Determining the Structural Ensembles of Disordered Protein States.Communications chemistry · 2020Article
- Information theoretic measures for quantifying sequence-ensemble relationships of intrinsically disordered proteins.Protein engineering, design & selection : PEDS · 2019Article
- Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Commonly used FRET fluorophores promote collapse of an otherwise disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Sequence Effects on Size, Shape, and Structural Heterogeneity in Intrinsically Disordered Proteins.The journal of physical chemistry. B · 2019Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
A mathematico-physically valid formulation is required to infer properties of disordered protein conformations from single-molecule Förster resonance energy transfer (smFRET). Conformational dimensions inferred by conventional approaches that presume a homogeneous conformational ensemble can be unphysical. When all possible-heterogeneous as well as homogeneous-conformational distributions are taken into account without prejudgment, a single value of average transfer efficiency 〈E〉 between dyes at two chain ends is generally consistent with highly diverse, multiple values of the average radius of gyration 〈R
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