ArticleNature communications2026
Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- AI-discovered protein fragments as generalizable regulators of biomolecular condensates.bioRxiv : the preprint server for biology · 2026Article
- Divergent effects of pathological α-synuclein truncations and mutations on phase separation.Nature communications · 2026Article
- Biomolecular Condensates Act as Distinct Solvation Environments That Reshape Amino Acid pJournal of the American Chemical Society · 2026Article
- Biomolecular Condensates Act as Distinct Solvation Environments that Reshape Amino Acid pKₐ Values.bioRxiv : the preprint server for biology · 2026Article
- Correlated Segments of Intrinsically Disordered Proteins as Drivers of Homotypic Phase Separation.JACS Au · 2025Article
- Amino acid transfer free energies reveal thermodynamic driving forces in biomolecular condensate formation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Prediction of phase-separation propensities of disordered proteins from sequence.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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Authors and funding
7 authors.
Funding
Abstract
Cellular organization in the form of biomolecular condensates is a fundamental regulatory mechanism across all forms of life. Formation of condensates relies on multivalent interactions that are often weak and transient, making them challenging to study experimentally. We have developed Condensate Partitioning by mRNA-Display (CPmD) to measure these interactions from the partition free energies of peptides and nucleic acids into reconstituted condensates. CPmD increases experimental throughput by several orders of magnitude, and we apply it to reveal the interactions driving condensate formation of intrinsically disordered proteins. We show that the partition free energies of about one hundred thousand peptides derived from the disordered proteome into a model condensate directly reflect their intrinsic propensity to form condensates. We reveal that amino acid content, linked to hydrophobicity, is the primary determinant of phase behavior. Additionally, CPmD uniquely resolves subtle sequence-dependent contributions that can encode specificity. CPmD thus provides a powerful tool to decipher how weak interactions between protein and RNA regulate biological function through condensate formation.
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