ArticleProceedings of the National Academy of Sciences of the United States of America2019
Commonly used FRET fluorophores promote collapse of an otherwise disordered protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 74 citations in OpenAlex.
- More Than a Glow: How Cyanine Dyes Shape Tracer Pharmacokinetics.Angewandte Chemie (International ed. in English) · 2026Review
- In Search of Shape in the Unshaped: Constructing Ensembles of Intrinsically Disordered Proteins.Biophysics reviews · 2026Article
- Time-Resolved SAXS Reveals Distinct Millisecond Metal-Induced Conformational Dynamics of Monomeric α-Synuclein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
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- Manifold of Polyampholyte Necklaces: From Charge Migration to Hierarchical Structure.Macromolecules · 2025Article
- Identification of an on-pathway intermediate illuminates the kinetic competition between protein folding and misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- AlphaFold prediction of structural ensembles of disordered proteins.Nature communications · 2025Article
- Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations.JACS Au · 2024Article
- Discovery of an on-pathway protein folding intermediate illuminates the kinetic competition between folding and misfolding.bioRxiv : the preprint server for biology · 2024Article
- 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
- Sequence-dependent conformational preferences of disordered single-stranded RNA.Cell reports. Physical science · 2024Article
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- Energy landscape of conformational changes for a single unmodified protein.Npj biosensing · 2024Article
- Ultraviolet Resonant Nanogap Antennas with Rhodium Nanocube Dimers for Enhancing Protein Intrinsic Autofluorescence.ACS nano · 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
- Factors That Control the Force Needed to Unfold a Membrane Protein in Silico Depend on the Mode of Denaturation.International journal of molecular sciences · 2023Article
- Effects of Sequence Composition, Patterning and Hydrodynamics on the Conformation and Dynamics of Intrinsically Disordered Proteins.International journal of molecular sciences · 2023Article
- The biophysics of disordered proteins from the point of view of single-molecule fluorescence spectroscopy.Essays in biochemistry · 2022Article
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Authors and funding
6 authors at 3 institutions in 1 country.
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Abstract
The dimensions that unfolded proteins, including intrinsically disordered proteins (IDPs), adopt in the absence of denaturant remain controversial. We developed an analysis procedure for small-angle X-ray scattering (SAXS) profiles and used it to demonstrate that even relatively hydrophobic IDPs remain nearly as expanded in water as they are in high denaturant concentrations. In contrast, as demonstrated here, most fluorescence resonance energy transfer (FRET) measurements have indicated that relatively hydrophobic IDPs contract significantly in the absence of denaturant. We use two independent approaches to further explore this controversy. First, using SAXS we show that fluorophores employed in FRET can contribute to the observed discrepancy. Specifically, we find that addition of Alexa-488 to a normally expanded IDP causes contraction by an additional 15%, a value in reasonable accord with the contraction reported in FRET-based studies. Second, using our simulations and analysis procedure to accurately extract both the radius of gyration (R
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