Evidence map›Paper›PMID 40455990›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Material properties of biomolecular condensates emerge from nanoscale dynamics.

Nicola Galvanetto, Miloš T Ivanović, Simone A Del Grosso, Aritra Chowdhury, Andrea Sottini, Daniel Nettels, Robert B Best, Benjamin Schuler

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed.

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  18. Non-Fickian diffusion within assemblies of the intrinsically disordered protein β-casein.Proceedings of the National Academy of Sciences of the United States of America · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Nicola GalvanettoDepartment of Biochemistry, University of Zurich, Zurich 8057, Switzerland.ORCID 0000-0002-0408-1747
Miloš T IvanovićDepartment of Biochemistry, University of Zurich, Zurich 8057, Switzerland.ORCID 0000-0003-3164-9411
Simone A Del GrossoDepartment of Biochemistry, University of Zurich, Zurich 8057, Switzerland.
Aritra ChowdhuryDepartment of Biochemistry, University of Zurich, Zurich 8057, Switzerland.ORCID 0000-0002-0579-292X
Andrea SottiniDepartment of Biochemistry, University of Zurich, Zurich 8057, Switzerland.
Daniel NettelsDepartment of Biochemistry, University of Zurich, Zurich 8057, Switzerland.
Robert B BestComputational Biophysics Section, Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.ORCID 0000-0002-7893-3543
Benjamin SchulerDepartment of Biochemistry, University of Zurich, Zurich 8057, Switzerland.ORCID 0000-0002-5970-4251

Funding

EC | Horizon Europe | Excellent Science | HORIZON EUROPE Marie Sklodowska-Curie Actions (MSCA) 898228Ernst Hadorn Foundation GalvanettoHHS | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK) Intramural Research ProgramNovo Nordisk Fonden (NNF) #NNF18OC0033926Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (SNF) 310030_197776
6 · The paper itself

Abstract

Biomolecular condensates form by phase separation of biological polymers and have important functions in the cell-functions that are inherently linked to their physical properties at different scales. A notable aspect of such membraneless organelles is that their viscoelastic properties can vary by orders of magnitude, but it has remained unclear how these pronounced differences are rooted in the nanoscale dynamics at the molecular level. Here, we investigate a series of condensates formed by complex coacervation of highly charged disordered proteins and polypeptides that span about two orders of magnitude in bulk viscosity. We find that their viscosity is highly correlated with protein translational diffusion and nano- to microsecond chain dynamics. Remarkably, analytical relations from polymer physics can predict condensate viscosity from diffusivity and chain dynamics, and vice versa, even for more hydrophobic disordered proteins and for synthetic polyelectrolytes, indicating a mechanistic link across several decades of length- and timescales. Atomistic simulations reveal that the observed differences in friction-a key quantity underlying these relations-reflect differences in interresidue contact lifetimes as a function of arginine content and salt concentration, leading to the vastly different dynamics among condensates. The rapid exchange of interresidue contacts we observe may be a general mechanism for preventing dynamic arrest in compartments densely packed with polyelectrolytes, such as the cell nucleus.

Indexed as

Biomolecular CondensatesPeptidesProteinsDiffusionHydrophobic and Hydrophilic InteractionsMolecular Dynamics SimulationViscosityPeptidesProteinsbiomolecular condensatescomplex coacervatesintrinsically disordered proteinsprotein dynamicsRouse model

Identifiers

PMID40455990
PMCPMC12167954

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Registered trials

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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.