ArticleProceedings of the National Academy of Sciences of the United States of America2012
Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 271 papers.
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271 citing papers in PubMed.
- Chain collapse, reduced dielectric, and water release drive protein phase separation.Biophysical journal · 2026Article
- Sequence determinants of the hypomobility of intrinsically disordered proteins in SDS-PAGE.Protein science : a publication of the Protein Society · 2026Article
- Red-to-Near-Infrared Fluorescence Resonance Energy Transfer Reporters for Dual Imaging Applications.Small methods · 2026Article
- Catalyst Hide-and-Seek Beneath Porous Support Surfaces: Pinpointing Active Site Distribution Through Resonance Energy Transfer.Angewandte Chemie (International ed. in English) · 2026Article
- Enzymatic Encoding of Topology in an Intrinsically Disordered Single-Chain Protein.Angewandte Chemie (International ed. in English) · 2026Article
- Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026Article
- In Search of Shape in the Unshaped: Constructing Ensembles of Intrinsically Disordered Proteins.Biophysics reviews · 2026Article
- The Polymers of Life: Exploring Cellular Function Through Polymer Concepts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Cooperativity, dynamics, and the free-energy surfaces of charge-patterned IDPs.bioRxiv : the preprint server for biology · 2026Article
- A 3D-Printed Scaffolded Hydrogel Microneedle Array Biosensor for Real-Time, Continuous Monitoring.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Hierarchical multi-timescale structural dynamics of the disordered N-terminal of p53.Nature communications · 2026Article
- Backbone rigidity of disordered protein linkers from NMR experiments and MD simulations.Biophysical journal · 2026Article
- Toward a unified framework for determining conformational ensembles of disordered proteins.Nature methods · 2026Review
- PEO-sheathed liquid jets increase sample delivery stability for serial femtosecond X-ray crystallography.Scientific reports · 2026Article
- Influence of Charge Block Length on Conformation and Cluster Formation of Atactic Peptide Polyampholytes.Macromolecules · 2026Article
- Residue-Specific Modulation of Aggregation-Associated Interactions by Spermine in Tau, α‑Synuclein, and Aβ40.JACS Au · 2026Article
- Backbone rigidity encodes universal viscoelastic signatures in biomolecular condensates.Biophysical journal · 2026Article
- Quantitative Integration of FRET and Molecular Dynamics for Modeling Flexible Peptides.The journal of physical chemistry. B · 2026Article
- Mapping Charge Interactions in Intrinsically Disordered Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Molecular origins of viscoelasticity in biomolecular condensates.The Journal of chemical physics · 2026Article
211 more citing papers are in PubMed but not listed here.
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6 authors.
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Abstract
The dimensions of unfolded and intrinsically disordered proteins are highly dependent on their amino acid composition and solution conditions, especially salt and denaturant concentration. However, the quantitative implications of this behavior have remained unclear, largely because the effective theta-state, the central reference point for the underlying polymer collapse transition, has eluded experimental determination. Here, we used single-molecule fluorescence spectroscopy and two-focus correlation spectroscopy to determine the theta points for six different proteins. While the scaling exponents of all proteins converge to 0.62 ± 0.03 at high denaturant concentrations, as expected for a polymer in good solvent, the scaling regime in water strongly depends on sequence composition. The resulting average scaling exponent of 0.46 ± 0.05 for the four foldable protein sequences in our study suggests that the aqueous cellular milieu is close to effective theta conditions for unfolded proteins. In contrast, two intrinsically disordered proteins do not reach the Θ-point under any of our solvent conditions, which may reflect the optimization of their expanded state for the interactions with cellular partners. Sequence analyses based on our results imply that foldable sequences with more compact unfolded states are a more recent result of protein evolution.
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