ArticleProceedings of the National Academy of Sciences of the United States of America2014
Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.
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Who cites it
120 citing papers in PubMed, 253 citations in OpenAlex.
- Biomolecular coacervation-mediated materials: Phase states, phase transitions, and biomedical applications.Bioactive materials · 2027Review
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- Engineering quantum dot surfaces to preserve protein-DNA interactions for single-molecule visualization.Nano convergence · 2026Article
- Glucose modulates macrophage polarization via glycating adsorbed albumin on titanium.Materials today. Bio · 2026Article
- Amyloid-β, Tau Protein, α-Synuclein, TDP-43, and FUS in Mixed Pathology: And Intrinsic Disorder to Rule Them All.International journal of molecular sciences · 2026Review
- Residue-level mapping of crowding effects on protein phase separation.Protein science : a publication of the Protein Society · 2026Article
- Protein structure and coupled solvent dynamics in α-synuclein fibrils under controlled confinement.Biophysical journal · 2026Article
- Using Multiple Isotope-Labeled Infrared Spectra for the Structural Characterization of an Intrinsically Disordered Peptide.The journal of physical chemistry. B · 2025Article
- Physical and Mechanical Properties of Monomeric Alpha-Synuclein Provide Leads to Molecular Function.The journal of physical chemistry. B · 2025Article
- A coarse-grained model for disordered proteins under crowded conditions.Protein science : a publication of the Protein Society · 2025Article
- PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025Article
- Scale-free Spatio-temporal Correlations in Conformational Fluctuations of Intrinsically Disordered Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Simulating Crowding In Vitro: Not an Elusive Goal Any Longer.Sub-cellular biochemistry · 2025Review
- Physics-Based Machine Learning Trains Hamiltonians and Decodes the Sequence-Conformation Relation in the Disordered Proteome.Journal of chemical theory and computation · 2024Article
- Disordered proteins interact with the chemical environment to tune their protective function during drying.eLife · 2024Article
- Core-shell model of the clusters of CPEB4 isoforms preceding liquid-liquid phase separation.Biophysical journal · 2024Article
- Hydrodynamic and thermodynamic analysis of PEGylated human serum albumin.Biophysical journal · 2024Article
- Peptide diffusion in biomolecular condensates.Biophysical journal · 2024Article
- Crowder titrations enable the quantification of driving forces for macromolecular phase separation.Biophysical journal · 2024Article
- Protecting Proteins from Desiccation Stress Using Molecular Glasses and Gels.Chemical reviews · 2024Review
60 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered proteins (IDPs) are involved in a wide range of regulatory processes in the cell. Owing to their flexibility, their conformations are expected to be particularly sensitive to the crowded cellular environment. Here we use single-molecule Förster resonance energy transfer to quantify the effect of crowding as mimicked by commonly used biocompatible polymers. We observe a compaction of IDPs not only with increasing concentration, but also with increasing size of the crowding agents, at variance with the predictions from scaled-particle theory, the prevalent paradigm in the field. However, the observed behavior can be explained quantitatively if the polymeric nature of both the IDPs and the crowding molecules is taken into account explicitly. Our results suggest that excluded volume interactions between overlapping biopolymers and the resulting criticality of the system can be essential contributions to the physics governing the crowded cellular milieu.
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