Evidence map›Paper›PMID 26112753›Full record

ArticleScientific reports2015

Spider wrapping silk fibre architecture arising from its modular soluble protein precursor.

Marie-Laurence Tremblay, Lingling Xu, Thierry Lefèvre, Muzaddid Sarker, Kathleen E Orrell, Jérémie Leclerc, Qing Meng, Michel Pézolet, Michèle Auger, Xiang-Qin Liu and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.5field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 50 citations in OpenAlex.

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  10. Aerodynamics and the role of the earth's electric field in the spiders' ballooning flight.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2021
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 2 countries.

Marie-Laurence TremblayDepartment of Biochemistry &Molecular Biology, Dalhousie University, Halifax, NS, Canada.
Lingling Xu1] Department of Biochemistry &Molecular Biology, Dalhousie University, Halifax, NS, Canada [2] Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai, P.R. China.
Thierry LefèvreDépartement de Chimie, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA) Université Laval, Québec, QC, Canada.
Muzaddid SarkerDepartment of Biochemistry &Molecular Biology, Dalhousie University, Halifax, NS, Canada.
Kathleen E OrrellDepartment of Biochemistry &Molecular Biology, Dalhousie University, Halifax, NS, Canada.
Jérémie LeclercDépartement de Chimie, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA) Université Laval, Québec, QC, Canada.
Qing MengInstitute of Biological Sciences and Biotechnology, Donghua University, Shanghai, P.R. China.
Michel PézoletDépartement de Chimie, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA) Université Laval, Québec, QC, Canada.
Michèle AugerDépartement de Chimie, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA) Université Laval, Québec, QC, Canada.
Xiang-Qin LiuDepartment of Biochemistry &Molecular Biology, Dalhousie University, Halifax, NS, Canada.
Jan K Rainey1] Department of Biochemistry &Molecular Biology, Dalhousie University, Halifax, NS, Canada [2] Department of Chemistry, Dalhousie University, Halifax, NS, Canada.
Dalhousie University · CAPROTEO · CAUniversité Laval · CADonghua University · CN

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Spiders store spidroins in their silk glands as high concentration aqueous solutions, spinning these dopes into fibres with outstanding mechanical properties. Aciniform (or wrapping) silk is the toughest spider silk and is devoid of the short amino acid sequence motifs characteristic of the other spidroins. Using solution-state NMR spectroscopy, we demonstrate that the 200 amino acid Argiope trifasciata AcSp1 repeat unit contrasts with previously characterized spidroins, adopting a globular 5-helix bundle flanked by intrinsically disordered N- and C-terminal tails. Split-intein-mediated segmental NMR-active isotope-enrichment allowed unambiguous demonstration of modular and malleable "beads-on-a-string" concatemeric behaviour. Concatemers form fibres upon manual drawing with silk-like morphology and mechanical properties, alongside secondary structuring and orientation consistent with native AcSp1 fibres. AcSp1 structural stability varies locally, with the fifth helix denaturing most readily. The structural transition of aciniform spidroin from a mostly α-helical dope to a mixed α-helix/β-sheet-containing fibre can be directly related to spidroin architecture and stability.

Indexed as

Amino Acid MotifsAnimalsDynamic Light ScatteringFibroinsHydrodynamicsInsect ProteinsNuclear Magnetic Resonance, BiomolecularProtein PrecursorsProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsSilkSpidersFibroinsInsect ProteinsProtein PrecursorsRecombinant Fusion ProteinsSilk

Identifiers

PMID26112753
PMCPMC4481645
OpenAlexW2413992581

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.