ArticleNature communications2018
Two-step self-assembly of a spider silk molecular clamp.
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 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Progress in Multiscale Modeling of Silk Materials.Biomacromolecules · 2024Review
- Structural conversion of the spidroin C-terminal domain during assembly of spider silk fibers.Nature communications · 2024Article
- The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection.Communications biology · 2024Article
- The role of flow in the self-assembly of dragline spider silk proteins.Biophysical journal · 2023Article
- Domain swap facilitates structural transitions of spider silk protein C-terminal domains.Protein science : a publication of the Protein Society · 2023Article
- Factors Influencing Properties of Spider Silk Coatings and Their Interactions within a Biological Environment.Journal of functional biomaterials · 2023Review
- Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk.Nature communications · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Web spiders synthesize silk fibers of unique strength and extensibility through the controlled self-assembly of protein building blocks, so-called spidroins. The spidroin C-terminal domain is highly conserved and connects two polypeptide chains through formation of an all-helical, intertwined dimer. Here we use contact-induced fluorescence self-quenching and resonance energy transfer in combination with far-UV circular dichroism spectroscopy as three orthogonal structural probes to dissect the mechanism of folding and dimerization of a spidroin C-terminal domain from the major ampullate gland of the nursery web spider Euprosthenops australis. We show that helices forming the dimer core assemble very rapidly and fold on association. Subsequently, peripheral helices fold and dock slowly onto the preformed core. Lability of outer helices facilitates formation of a highly expanded, partially folded dimer. The high end-to-end distance of chain termini in the partially folded dimer suggests an extensibility module that contributes to elasticity of spider silk.
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Registered trials
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