ArticleACS macro letters2023
Conformational Properties of Polymers at Droplet Interfaces as Model Systems for Disordered Proteins.
Article in ACS macro letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 36 citations in OpenAlex.
- Biomolecular Condensates Act as Distinct Solvation Environments That Reshape Amino Acid pJournal of the American Chemical Society · 2026Article
- Origin of the ionic-strength dependent reentrant behavior in the liquid-liquid phase separation of uncharged intrinsically disordered proteins.Communications chemistry · 2026Article
- Sticky interactions govern sequence-dependent dynamics in biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Biomolecular condensate microstructure is invariant to sequence-encoded molecular and macroscopic properties.Soft matter · 2025Article
- Differential conformational expansion of NUP98-HOXA9 oncoprotein from nanosized assemblies to macrophases.Nature communications · 2025Article
- Current practices in the study of biomolecular condensates: a community comment.Nature communications · 2025Article
- Via entropy analysis (EA) and systematic cluster analysis (SCA), multi-index chemometric analysis of 20 amino acids, trace elements, etc., of five green teas from Guizhou, China.BMC chemistry · 2025Article
- Biomolecular condensate microstructure couples molecular and mesoscale properties.bioRxiv : the preprint server for biology · 2025Article
- Expanding the molecular grammar of polar residues and arginine in FUS phase separation.Nature chemical biology · 2025Article
- Sequence-encoded intermolecular base pairing modulates fluidity in DNA and RNA condensates.Nature communications · 2025Article
- Backbone-mediated weakening of pairwise interactions enables percolation in peptide-based mimics of protein condensates.Communications chemistry · 2025Article
- Size-controlled assembly of phase separated protein condensates with interfacial protein cages.Nature communications · 2025Article
- Prion and "Prion-Like" Detection: From Conventional Methods to Microfluidics or Lab-on-Chip Platforms to Monitor Seeding and Spreading of Misfolded Proteins.Sub-cellular biochemistry · 2025Review
- Sequence-Encoded Spatiotemporal Dependence of Viscoelasticity of Protein Condensates Using Computational Microrheology.JACS Au · 2024Article
- The conformations of protein chains at the interface of biomolecular condensates.Nature communications · 2024Article
- Article
- Direct computations of viscoelastic moduli of biomolecular condensates.The Journal of chemical physics · 2024Article
- Sequence-encoded Spatiotemporal Dependence of Viscoelasticity of Protein Condensates Using Computational Microrheology.bioRxiv : the preprint server for biology · 2024Article
- Insights into Molecular Diversity within the FUS/EWS/TAF15 Protein Family: Unraveling Phase Separation of the N-Terminal Low-Complexity Domain from RNA-Binding Protein EWS.Journal of the American Chemical Society · 2024Article
- Expanding the molecular grammar of polar residues and arginine in FUS prion-like domain phase separation and aggregation.bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
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Abstract
Polymer models serve as useful tools for studying the formation and physical properties of biomolecular condensates. In recent years, the interface dividing the dense and dilute phases of condensates has been discovered to be closely related to their functionality, but the conformational preferences of the constituent proteins remain unclear. To elucidate this, we perform molecular simulations of a droplet formed by phase separation of homopolymers as a surrogate model for the prion-like low-complexity domains. By systematically analyzing the polymer conformations at different locations in the droplet, we find that the chains become compact at the droplet interface compared with the droplet interior. Further, segmental analysis revealed that the end sections of the chains are enriched at the interface to maximize conformational entropy and are more expanded than the middle sections of the chains. We find that the majority of chain segments lie tangential to the droplet surface, and only the chain ends tend to align perpendicular to the interface. These trends also hold for the natural proteins FUS LC and LAF-1 RGG, which exhibit more compact chain conformations at the interface compared to the droplet interior. Our findings provide important insights into the interfacial properties of biomolecular condensates and highlight the value of using simple polymer physics models to understand the underlying mechanisms.
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