ArticleProceedings of the National Academy of Sciences of the United States of America2025
Arg-Tyr cation-π interactions drive phase separation and β-sheet assembly in native spider dragline silk.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Diverging Liquid-Liquid Phase Separation Behavior of Different Recombinant Major Ampullate Spidroins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- MOFF2: A Transferable Coarse-Grained Protein Force Field for Predictive Condensate Simulations.bioRxiv : the preprint server for biology · 2026Article
- Silk-Inspired Design and Manufacturing of Robust Plantymers.Nature communications · 2026Article
- A Systematic Evaluation of Protein Phase Separation Predictors across Diverse Protein Landscapes.Computational and structural biotechnology journal · 2026Article
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Authors and funding
14 authors.
Funding
Abstract
Liquid-liquid phase separation (LLPS) is a fundamental principle of protein organization in intrinsically disordered proteins (IDPs) and biomaterials, yet the residue-level interactions that link condensation to structural ordering remain poorly defined. In spider dragline silk, LLPS is believed to initiate the transition from soluble spidroin dope into β-sheet-rich fibers that provide exceptional toughness, yet how sequence-specific motifs govern this process has been unclear. Here, we combine isotope-edited solution NMR, dynamic nuclear polarization (DNP)-enhanced solid-state NMR, molecular dynamics simulations, and AlphaFold3 modeling to define the molecular role of arginine and tyrosine in
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