ArticleNature communications2018
Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Silk-Inspired Design and Manufacturing of Robust Plantymers.Nature communications · 2026Article
- Phosphate- and pH-dependent self-assembly of recombinant spider silk proteins.Protein science : a publication of the Protein Society · 2026Article
- Spider silk-based structural proteins as tough, biodegradable, and sustainable polymers.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2026Review
- Nanostructured Protein Surfaces Inspired by Spider Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- Sequence-encoded tubular architectures in disordered spider silk proteins revealed by multiscale simulations and NMR.PNAS nexus · 2025Article
- Physics-informed deep learning for plasmonic sensing of nanoscale protein dynamics in solution.Science advances · 2025Article
- Manipulating the Assembly and Architecture of Fibrillar Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Functional Biomaterials Derived from Protein Liquid-Liquid Phase Separation and Liquid-to-Solid Transition.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- The Biology of Natural Polymers Accelerates and Expands the Science of Biomacromolecules: A Focus on Structural Proteins.Biomacromolecules · 2025Review
- Design and applications of self-assembled polypeptide matrices in wound healing.Frontiers in bioengineering and biotechnology · 2025Review
- Rapid Interpretation of Protein Backbone Rotation Dynamics Directly from Spin Relaxation Data.The journal of physical chemistry letters · 2024Article
- Tuning the viscoelastic properties of peptide coacervates by single amino acid mutations and salt kosmotropicity.Communications chemistry · 2024Article
- The role of flow in the self-assembly of dragline spider silk proteins.Biophysical journal · 2023Article
- Unusual pBiomacromolecules · 2023Article
- A brief review on the mechanisms and approaches of silk spinning-inspired biofabrication.Frontiers in bioengineering and biotechnology · 2023Review
- Complexity of Spider Dragline Silk.Biomacromolecules · 2022Review
- Seeking Solvation: Exploring the Role of Protein Hydration in Silk Gelation.Molecules (Basel, Switzerland) · 2022Article
- Presence of β-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR.Molecules (Basel, Switzerland) · 2022Article
- A targeted bioinformatics approach identifies highly variable cell surface proteins that are unique to Glomeromycotina.Mycorrhiza · 2022Article
- Accurate Machine Learning Prediction of Protein Circular Dichroism Spectra with Embedded Density Descriptors.JACS Au · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The β-sheet is the key structure underlying the excellent mechanical properties of spider silk. However, the comprehensive mechanism underlying β-sheet formation from soluble silk proteins during the transition into insoluble stable fibers has not been elucidated. Notably, the assembly of repetitive domains that dominate the length of the protein chains and structural features within the spun fibers has not been clarified. Here we determine the conformation and dynamics of the soluble precursor of the repetitive domain of spider silk using solution-state NMR, far-UV circular dichroism and vibrational circular dichroism. The soluble repetitive domain contains two major populations: ~65% random coil and ~24% polyproline type II helix (PPII helix). The PPII helix conformation in the glycine-rich region is proposed as a soluble prefibrillar region that subsequently undergoes intramolecular interactions. These findings unravel the mechanism underlying the initial step of β-sheet formation, which is an extremely rapid process during spider silk assembly.
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