ArticleThe journal of physical chemistry. B2021
Biophysics of Phase Separation of Disordered Proteins Is Governed by Balance between Short- And Long-Range Interactions.
Article in The journal of physical chemistry. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed.
- Article
- Mapping interactions between disordered regions reveals promiscuity in biomolecular condensate formation.Nature communications · 2026Article
- How the Extent of Protein Folding and Oligomerization Modulate Condensate Formation and Properties.The journal of physical chemistry letters · 2025Article
- Role of Charge Patterning and Hydrophobicity in Peptide-Based Complex Coacervates.Biomacromolecules · 2025Article
- Multivalent interaction induces phase separation and formation of more toxic aggregates of α-syn in a yeast model of Parkinson's disease.Protein science : a publication of the Protein Society · 2025Article
- Glycosylation Weakens Skp1 Homodimerization inBiochemistry · 2025Article
- Interplay of Hydrophobicity, Charge, and Sequence Length in Oligopeptide Coassembly.The journal of physical chemistry. B · 2025Article
- Backbone-mediated weakening of pairwise interactions enables percolation in peptide-based mimics of protein condensates.Communications chemistry · 2025Article
- Interaction-Dependent Secondary Structure of Peptides in Biomolecular Condensates.Journal of the American Chemical Society · 2024Article
- SHARK enables sensitive detection of evolutionary homologs and functional analogs in unalignable and disordered sequences.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Peptide diffusion in biomolecular condensates.Biophysical journal · 2024Article
- Direct prediction of intermolecular interactions driven by disordered regions.bioRxiv : the preprint server for biology · 2024Article
- Active learning of the thermodynamics-dynamics trade-off in protein condensates.Science advances · 2024Article
- Ultrafast Spectroscopy Reveals Slow Water Dynamics in Biocondensates.Journal of the American Chemical Society · 2023Article
- Cross-Talk of Cation-π Interactions with Electrostatic and Aromatic Interactions: A Salt-Dependent Trade-off in Biomolecular Condensates.The journal of physical chemistry letters · 2023Article
- Developments in describing equilibrium phase transitions of multivalent associative macromolecules.Current opinion in structural biology · 2023Review
- Conformational Analysis of Charged Homo-Polypeptides.Biomolecules · 2023Article
- Biomolecular condensates formed by designer minimalistic peptides.Nature communications · 2023Article
- Condensates formed by prion-like low-complexity domains have small-world network structures and interfaces defined by expanded conformations.Nature communications · 2022Article
- Multi-level analysis of intrinsically disordered protein docking methods.Methods (San Diego, Calif.) · 2022Article
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2 authors.
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Abstract
Intrinsically disordered proteins play a crucial role in cellular phase separation, yet the diverse molecular forces driving phase separation are not fully understood. It is of utmost importance to understand how peptide sequence, and particularly the balance between the peptides' short- and long-range interactions with other peptides, may affect the stability, structure, and dynamics of liquid-liquid phase separation in protein condensates. Here, using coarse-grained molecular dynamics simulations, we studied the liquid properties of the condensate in a series of polymers in which the ratio of short-range dispersion interactions to long-range electrostatic interactions varied. As the fraction of mutations that participate in short-range interactions increases at the expense of long-range electrostatic interactions, a significant decrease in the critical temperature of phase separation is observed. Nevertheless, sequences with a high fraction of short-range interactions exhibit stabilization, which suggests compensation for the loss of long-range electrostatic interactions. Decreased condensate stability is coupled with decreased translational diffusion of the polymers in the condensate, which may result in the loss of liquid characteristics in the presence of a high fraction of uncharged residues. The effect of exchanging long-range electrostatic interactions for short-range interactions can be explained by the kinetics of breaking intermolecular contacts with neighboring polymers and the kinetics of intramolecular fluctuations. While both time scales are coupled and increase as electrostatic interactions are lost, for sequences that are dominated by short-range interactions, the kinetics of intermolecular contact breakage significantly slows down. Our study supports the contention that different types of interactions can maintain protein condensates, however, long-range electrostatic interactions enhance its liquid-like behavior.
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