ArticleMacromolecules2022
Effect of Charge Distribution on the Dynamics of Polyampholytic Disordered Proteins.
Article in Macromolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Cooperativity, dynamics, and the free-energy surfaces of charge-patterned IDPs.bioRxiv : the preprint server for biology · 2026Article
- Intrinsic Disorder as a Biomimetic Design Paradigm.Biomimetics (Basel, Switzerland) · 2026Article
- Dilute but Dense - Reversible Crosslinking Enables Water-Rich (Bio)polymer Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Sequence and length-scale dependent dynamics in biocondensates of highly charged 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
- Polymerization-mediated SRFR1 condensation in upper lateral root cap cells regulates root growth.The Plant cell · 2026Article
- Multiphasic Organization and Differential Dynamics of Proteins within Protein-DNA Biomolecular Condensates.The journal of physical chemistry. B · 2025Article
- Manifold of Polyampholyte Necklaces: From Charge Migration to Hierarchical Structure.Macromolecules · 2025Article
- Biomolecular phase separation in tumorigenesis: from aberrant condensates to therapeutic vulnerabilities.Molecular cancer · 2025Review
- Context-dependent effect of polyethylene glycol on the structure and dynamics of hirudin.Biophysical journal · 2025Article
- Sequence-Encoded Spatiotemporal Dependence of Viscoelasticity of Protein Condensates Using Computational Microrheology.JACS Au · 2024Article
- Sequence-encoded Spatiotemporal Dependence of Viscoelasticity of Protein Condensates Using Computational Microrheology.bioRxiv : the preprint server for biology · 2024Article
- Determinants that enable disordered protein assembly into discrete condensed phases.Nature chemistry · 2024Article
- Expanding the molecular language of protein liquid-liquid phase separation.Nature chemistry · 2024Article
- Effects of Charge Sequence Pattern and Lysine-to-Arginine Substitution on the Structural Stability of Bioinspired Polyampholytes.Biomacromolecules · 2024Article
- HYPK: A marginally disordered protein sensitive to charge decoration.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Sequence-dependent material properties of biomolecular condensates and their relation to dilute phase conformations.Nature communications · 2024Article
- Sequence-Dependent Material Properties of Biomolecular Codensates and their Relation to Dilute Phase Conformations.bioRxiv : the preprint server for biology · 2024Article
- Sequence-Dependent Conformational Transitions of Disordered Proteins During Condensation.bioRxiv : the preprint server for biology · 2024Article
- Conformational Properties of Polymers at Droplet Interfaces as Model Systems for Disordered Proteins.ACS macro letters · 2023Article
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Authors and funding
6 authors.
Funding
Abstract
The stability and physiological function of many biomolecular coacervates depend on the structure and dynamics of intrinsically disordered proteins (IDPs) that typically contain a significant fraction of charged residues. Although the effect of relative arrangement of charged residues on IDP conformation is a well-studied problem, the associated changes in dynamics are far less understood. In this work, we systematically interrogate the effects of charge distribution on the chain-level and segmental dynamics of polyampholytic IDPs in dilute solutions. We study a coarse-grained model polyampholyte consisting of an equal fraction of two oppositely charged residues (glutamic acid and lysine) that undergoes a transition from an ideal chain-like conformation for uniformly charge-patterned sequences to a semi-compact conformation for highly charge-segregated sequences. Changes in the chain-level dynamics with increasing charge segregation correlate with changes in conformation. The chain-level and segmental dynamics conform to simple homopolymer models for uniformly charge-patterned sequences but deviate with increasing charge segregation, both in the presence and absence of hydrodynamic interactions. We discuss the significance of these findings, obtained for a model polyampholyte, in the context of a charge-rich intrinsically disordered region of the naturally occurring protein LAF-1. Our findings have important implications for understanding the effects of charge patterning on the dynamics of polyampholytic IDPs in dilute conditions using polymer scaling theories.
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