ArticleScientific reports2017
Conservation of folding and association within a family of spidroin N-terminal domains.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Ultratight Binding of a Capture Spiral Spider Silk Protein through Electrostatic Forces.ACS bio & med chem Au · 2026Article
- Intrinsically disordered linkers and terminal domains codrive aciniform spidroin self-assembly through liquid-liquid phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Domain swap facilitates structural transitions of spider silk protein C-terminal domains.Protein science : a publication of the Protein Society · 2023Article
- The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence.The Journal of biological chemistry · 2022Article
- Solution Structure of Tubuliform Spidroin N-Terminal Domain and Implications for pH Dependent Dimerization.Frontiers in molecular biosciences · 2022Article
- Critical role of minor eggcase silk component in promoting spidroin chain alignment and strong fiber formation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Advances in Plant-Derived Scaffold Proteins.Frontiers in plant science · 2020Review
- Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk.Nature communications · 2019Article
- Two-step self-assembly of a spider silk molecular clamp.Nature communications · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Web spiders synthesize silk fibres, nature's toughest biomaterial, through the controlled assembly of fibroin proteins, so-called spidroins. The highly conserved spidroin N-terminal domain (NTD) is a pH-driven self-assembly device that connects spidroins to super-molecules in fibres. The degree to which forces of self-assembly is conserved across spider glands and species is currently unknown because quantitative measures are missing. Here, we report the comparative investigation of spidroin NTDs originating from the major ampullate glands of the spider species Euprosthenops australis, Nephila clavipes, Latrodectus hesperus, and Latrodectus geometricus. We characterized equilibrium thermodynamics and kinetics of folding and self-association using dynamic light scattering, stopped-flow fluorescence and circular dichroism spectroscopy in combination with thermal and chemical denaturation experiments. We found cooperative two-state folding on a sub-millisecond time scale through a late transition state of all four domains. Stability was compromised by repulsive electrostatic forces originating from clustering of point charges on the NTD surface required for function. pH-driven dimerization proceeded with characteristic fast kinetics yielding high affinities. Results showed that energetics and kinetics of NTD self-assembly are highly conserved across spider species despite the different silk mechanical properties and web geometries they produce.
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