ArticleChemical science2024
Sequence-dependent conformational transitions of disordered proteins during condensation.
Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Article
- The emerging synergy of experimental and computational approaches for therapeutic modulation of biomolecular condensates.SLAS discovery : advancing life sciences R & D · 2026Review
- Condensates as Conformation Editors of Disordered Client Proteins.Journal of the American Chemical Society · 2026Article
- Folded domains impose structural heterogeneity and attenuated dynamics in biomolecular condensates.Nature communications · 2026Article
- Backbone rigidity encodes universal viscoelastic signatures in biomolecular condensates.Biophysical journal · 2026Article
- Density transitions in the regulation of transcription.Molecular cell · 2026Review
- Molecular origins of viscoelasticity in biomolecular condensates.The Journal of chemical physics · 2026Article
- Sticky interactions govern sequence-dependent dynamics in biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Controlling interfacial protein adsorption, desorption and aggregation in biomolecular condensates.Nature communications · 2025Article
- 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
- A molecular census to elucidate the demixing mechanism of membraneless organelles.Genome biology · 2025Article
- Biomolecular condensate viscoelasticity is dictated by the interplay between single-molecule shape memory and mesh reconfigurability.bioRxiv : the preprint server for biology · 2025Article
- Elucidation of the Molecular Interaction Network Underlying Full-Length FUS Conformational Transitions and Its Phase Separation Using Atomistic Simulations.The journal of physical chemistry. B · 2025Article
- Current practices in the study of biomolecular condensates: a community comment.Nature communications · 2025Article
- Structural and Functional Relevance of Charge-Based Transient Interactions inside Intrinsically Disordered Proteins.ACS physical chemistry Au · 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 Spatiotemporal Dependence of Viscoelasticity of Protein Condensates Using Computational Microrheology.JACS Au · 2024Article
- Structural and Functional Relevance of Charge Based Transient Interactions inside Intrinsically Disordered Proteins.bioRxiv : the preprint server for biology · 2024Article
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Abstract
Intrinsically disordered proteins (IDPs) can form biomolecular condensates through phase separation. It is recognized that the conformation of IDPs in the dense and dilute phases, as well as at the interfaces of condensates, can critically impact their functionality. However, a residue-level understanding of the conformational transitions of IDPs during condensation remains elusive. In this study, we employ a coarse-grained polyampholyte model, comprising an equal number of oppositely charged residues-glutamic acid and lysine-whereby conformations and phase behavior can be tuned by altering the protein sequence. By manipulating sequence patterns from perfectly alternating to block-like, we obtain chains with ideal-like conformations to semi-compact structures in the dilute phase. In the dense phase, however, the chain conformation approaches that of an ideal chain, regardless of the sequence. Simulations across different concentrations reveal that chains transition from small oligomeric clusters in the dilute phase to the dense phase, with a gradual swelling of individual chains. These findings are further validated with naturally occurring protein sequences involved in biological condensate formation. Additionally, we show that chain conformations at the interface display a strong sequence dependence, remaining more collapsed than those in the bulk-like dense phase. This study provides detailed insights into how the conformations of a specific subclass of IDPs (lacking secondary structures) change within condensates and in solution, as governed by their sequences.
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