ArticleProceedings of the National Academy of Sciences of the United States of America2020
Depletion interactions modulate the binding between disordered proteins in crowded environments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 151 citations in OpenAlex.
- Holographic Fingerprinting Reveals Oligomer-Driven Phase Separation in Bovine Serum Albumin.Chemical & biomedical imaging · 2026Article
- Advancements in single-molecule fluorescence spectroscopy for probing conformations, dynamics, and interactions in disordered protein regions.Current opinion in structural biology · 2026Review
- Too close for comfort: Self-crowding transforms protein structure and stability beyond volume exclusion.Protein science : a publication of the Protein Society · 2026Article
- How Binding Affinity and Binding Specificity Map to Sequence Space.Journal of molecular evolution · 2026Article
- Toward a unified framework for determining conformational ensembles of disordered proteins.Nature methods · 2026Review
- Residue-level mapping of crowding effects on protein phase separation.Protein science : a publication of the Protein Society · 2026Article
- Lipoprotein diffusion in dense yolk plasma is governed by softness, hydrodynamics, and caging: Insights from MHz-XPCS.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The human RAD52 complex undergoes phase separation and facilitates bundling and end-to-end tethering of RAD51 presynaptic filaments.Nucleic acids research · 2026Article
- A Facile Platform for One-Step Generation of Uniform Microdroplets through Dehydration-Driven Phase Separation in Microfluidics.Small methods · 2026Article
- Glycopolymers stabilize protein folding and protein-protein interactions via enthalpic interactions.Protein science : a publication of the Protein Society · 2026Article
- A cautious user's guide in applying HMMs to physical systems.The Journal of chemical physics · 2025Article
- Osmotic pressure regulates DNA labelling and transcription with dCas9-SunTag system in live cells.Nature communications · 2025Article
- Repulsive vs Attractive Crowding Distinctly Regulate TDP-43 Condensates through Region-specific Structural Dynamics.JACS Au · 2025Article
- Reversible Bacterial Depletion Aggregation and Restabilization by Water-Soluble Polymers.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Foundation model for efficient biological discovery in single-molecule time traces.Nature methods · 2025Article
- A coarse-grained model for disordered proteins under crowded conditions.Protein science : a publication of the Protein Society · 2025Article
- Crowding beyond excluded volume: A tale of two dimers.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
- Accelerated amyloid fibril formation at the interface of liquid-liquid phase-separated droplets by depletion interactions.Protein science : a publication of the Protein Society · 2025Article
- Microenvironment-confined kinetic elucidation and implementation of a DNA nano-phage with a shielded internal computing layer.Nature communications · 2025Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered proteins (IDPs) abound in cellular regulation. Their interactions are often transitory and highly sensitive to salt concentration and posttranslational modifications. However, little is known about the effect of macromolecular crowding on the interactions of IDPs with their cellular targets. Here, we investigate the influence of crowding on the interaction between two IDPs that fold upon binding, with polyethylene glycol as a crowding agent. Single-molecule spectroscopy allows us to quantify the effects of crowding on a comprehensive set of observables simultaneously: the equilibrium stability of the complex, the association and dissociation kinetics, and the microviscosity, which governs translational diffusion. We show that a quantitative and coherent explanation of all observables is possible within the framework of depletion interactions if the polymeric nature of IDPs and crowders is incorporated based on recent theoretical developments. The resulting integrated framework can also rationalize important functional consequences, for example, that the interaction between the two IDPs is less enhanced by crowding than expected for folded proteins of the same size.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.