ArticleCurrent research in structural biology2021
Folded domain charge properties influence the conformational behavior of disordered tails.
Article in Current research in structural biology, 2021. 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, 41 citations in OpenAlex.
- Fluorescent protein and peptide tags alter condensate formation and dynamics in vivo and in vitro.EMBO reports · 2026Article
- How the Extent of Protein Folding and Oligomerization Modulate Condensate Formation and Properties.The journal of physical chemistry letters · 2025Article
- Insights into Noncanonical and Diversified Functions of ABCF1: From Health to Disease.Journal of molecular biology · 2025Review
- A Charge-Driven Strategy for Covalent Modification and Modulation of Biomolecular Condensates.Journal of the American Chemical Society · 2025Article
- Martini3-IDP: improved Martini 3 force field for disordered proteins.Nature communications · 2025Article
- The role of intrinsically disordered regions of SARS-CoV-2 nucleocapsid and non-structural protein 1 proteins.Frontiers in chemistry · 2025Review
- A coarse-grained model for disordered and multi-domain proteins.Protein science : a publication of the Protein Society · 2024Article
- Acetylation-Dependent Compaction of the Histone H4 Tail Ensemble.The journal of physical chemistry. B · 2024Article
- Conserved molecular recognition by an intrinsically disordered region in the absence of sequence conservation.Research square · 2024Article
- HYPK: A marginally disordered protein sensitive to charge decoration.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Interplay between charge distribution and DNA in shaping HP1 paralog phase separation and localization.eLife · 2024Article
- The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA.Nucleic acids research · 2024Article
- Direct prediction of intrinsically disordered protein conformational properties from sequence.Nature methods · 2024Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- DNA binding redistributes activation domain ensemble and accessibility in pioneer factor Sox2.Nature communications · 2024Article
- Structural biases in disordered proteins are prevalent in the cell.Nature structural & molecular biology · 2024Article
- A complex network of interdomain interactions underlies the conformational ensemble of monomeric TDP-43 and modulates its phase behavior.Protein science : a publication of the Protein Society · 2024Article
- Article
- Structural Preferences Shape the Entropic Force of Disordered Protein Ensembles.The journal of physical chemistry. B · 2023Article
- Structural preferences shape the entropic force of disordered protein ensembles.bioRxiv : the preprint server for biology · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered proteins and protein regions (IDRs) make up around 30% of the human proteome where they play essential roles in dictating and regulating many core biological processes. While IDRs are often studied as isolated domains, in naturally occurring proteins most IDRs are found adjacent to folded domains, where they exist as either N- or C-terminal tails or as linkers connecting two folded domains. Prior work has shown that charge properties of IDRs can influence their conformational behavior, both in isolation and in the context of folded domains. In contrast, the converse scenario is less well-explored: how do the charge properties of folded domains influence IDR conformational behavior? To answer this question, we combined a large-scale structural bioinformatics analysis with all-atom implicit solvent simulations of both rationally designed and naturally occurring proteins. Our results reveal three key takeaways. Firstly, the relative position and accessibility of charged residues across the surface of a folded domain can dictate IDR conformational behavior, overriding expectations based on net surface charge properties. Secondly, naturally occurring proteins possess multiple charge patches that are physically accessible to local IDRs. Finally, even modest changes in the local electrostatic environment of a folded domain can substantially modulate IDR-folded domain interactions. Taken together, our results suggest that folded domain surfaces can act as local determinants of IDR conformational behavior.
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