ArticleProceedings of the National Academy of Sciences of the United States of America2022
Competing interactions give rise to two-state behavior and switch-like transitions in charge-rich intrinsically disordered proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- Electrostatic-Hydrophobic Competition Induces Re-Entrant Phase Separation in Designer Polypeptides.ACS omega · 2026Article
- Beyond the structure-function paradigm: A comprehensive review of intrinsically disordered proteins.Biochemistry and biophysics reports · 2026Review
- Multisite Threonine Phosphorylation in the SPT5 C-Terminal Region 1 Enables Sequence-Dependent Regulation without Global Structural Remodeling.The journal of physical chemistry. B · 2026Article
- The role of the 2'-OH group in phase separation and percolation transitions of RNA.Nature communications · 2026Article
- Structural Features of a Tiny Viral Protein, ORF7b of SARS-CoV-2.International journal of molecular sciences · 2026Article
- The Critical Role of the 2'-OH group in Phase Separation and Percolation Transitions of RNA.bioRxiv : the preprint server for biology · 2026Article
- Cooperativity, dynamics, and the free-energy surfaces of charge-patterned IDPs.bioRxiv : the preprint server for biology · 2026Article
- Asymmetry in Hydrophobicity Induces Electric Potential in Non-Charged Biomolecular Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Manifold of Polyampholyte Necklaces: From Charge Migration to Hierarchical Structure.Macromolecules · 2025Article
- Size, Conformation, and Local Domains of Single-Chain Nanoparticles with Intrachain Covalent, Dipolar, and Electrostatic Interactions: Toward Artificial Intrinsically Disordered Proteins.Macromolecules · 2025Article
- Structural and Functional Relevance of Charge-Based Transient Interactions inside Intrinsically Disordered Proteins.ACS physical chemistry Au · 2025Article
- Synapsin Condensation is Governed by Sequence-Encoded Molecular Grammars.Journal of molecular biology · 2025Article
- Article
- CaProtein science : a publication of the Protein Society · 2025Article
- Molecular insights into the interaction between a disordered protein and a folded RNA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Emergent microenvironments of nucleoli.Nucleus (Austin, Tex.) · 2024Review
- Structural and Functional Relevance of Charge Based Transient Interactions inside Intrinsically Disordered Proteins.bioRxiv : the preprint server for biology · 2024Article
- Beyond monopole electrostatics in regulating conformations of intrinsically disordered proteins.PNAS nexus · 2024Article
- CytochromeiScience · 2024Article
- Molecular insights into the interaction between a disordered protein and a folded RNA.bioRxiv : the preprint server for biology · 2024Article
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3 authors.
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Abstract
The most commonly occurring intrinsically disordered proteins (IDPs) are polyampholytes, which are defined by the duality of low net charge per residue and high fractions of charged residues. Recent experiments have uncovered nuances regarding sequence–ensemble relationships of model polyampholytic IDPs. These include differences in conformational preferences for sequences with lysine vs. arginine and the suggestion that well-mixed sequences form a range of conformations, including globules, conformations with ensemble averages that are reminiscent of ideal chains, or self-avoiding walks. Here, we explain these observations by analyzing results from atomistic simulations. We find that polyampholytic IDPs generally sample two distinct stable states, namely, globules and self-avoiding walks. Globules are favored by electrostatic attractions between oppositely charged residues, whereas self-avoiding walks are favored by favorable free energies of hydration of charged residues. We find sequence-specific temperatures of bistability at which globules and self-avoiding walks can coexist. At these temperatures, ensemble averages over coexisting states give rise to statistics that resemble ideal chains without there being an actual counterbalancing of intrachain and chain-solvent interactions. At equivalent temperatures, arginine-rich sequences tilt the preference toward globular conformations whereas lysine-rich sequences tilt the preference toward self-avoiding walks. We also identify differences between aspartate- and glutamate-containing sequences, whereby the shorter aspartate side chain engenders preferences for metastable, necklace-like conformations. Finally, although segregation of oppositely charged residues within the linear sequence maintains the overall two-state behavior, compact states are highly favored by such systems.
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