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8 results for “silk production”

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dryad36/100

Rapid mid-jump production of high-performance silk by jumping spiders

<p><span><span><span><span><span><span><span><span><span><span>Jumping spiders (Salticidae) do not rely on webs to capture their prey, but they do spin a silk dragline behind them as they move through their habitat. They also spin this dragline during jumps, continuously connecting them with the surface they leapt<b> </b>from. Since spiders cannot spin silk in advance, this silk must be spun at the same speed as the spider jumps—in effect, requiring spin speeds over ten times faster than typical. And while many spiders can move rapidly (e.g. running or rappelling), previous research on silk has found that silk spinning rates in excess of walking and web-building speeds (~2-20mm/s) result in lower quality silk and even dragline failure. Here we found that despite being spun at high speeds (~500-700mm/s; 100-140 body lengths/s), jump-spun salticid silk showed consistent, uniform structure as well as the high-performance qualities characteristic of silk spun by other spiders, including orb-weaving species, at low speeds. Toughness of this jump-spun silk (mean = 281.9MJ/m<sup>3</sup>) even surpassed reported values for all but the toughest orb-web draglines. This provides the first evidence that salticids are capable of spinning high-performance silk and are able to do so extremely rapidly under natural conditions.</span></span></span></span></span></span></span></span></span></span></p>

opencc-zeroNov 2021View details →
dryad36/100

Rapid mid-jump production of high-performance silk by jumping spiders

Open the record for dataset details and reuse information.

publicNov 2021View details →
zenodo28/100

Data for "Metal Ions Guide the Production of Silkworm Silk Fibers"

Open the record for dataset details and reuse information.

opencc-by-4.0Jun 2024View details →
zenodo28/100

Figure 3 from: Molino J, Lubiana Alves T, Ferreira-Camargo L, Croce M, Tanaka A, Buson F, Ribeiro P, Campos-Salazar A, Antonio E, Maizel A, Siratuti V, Costa C, Wlodarczyk S, de Souza Lima R, Mello F, Mayfield S, Carvalho J (2016) Chimeric spider silk production in microalgae: a modular bionanomaterial. Research Ideas and Outcomes 2: e9342. https://doi.org/10.3897/rio.2.e9342

Figure 3 - Cassette construction to be inserted in C. renhardtii nuclear genome for the expression of desired proteins. Promoter hsp70A/rbcs2: fusion of the promoters hsp70A and rbcs2 (Eichler-Stahlberg et al. 2009, Schroda et al. 2000). Sh-Ble: gene that gives resistance to Zeomycin. 2A: self-cleavage peptide obtained from Foot and Mouth Disease Virus (FMDV) (Rasala et al. 2012). PS: Secretion signal peptide of the gene Ars1. GOI: gene of interest coding the proteins to be used in the project. His: coding sequence of six histidines (histidine tag). RbcS2 3'UTR: terminal sequence (untranslated region) of the gene RbcS2 (Fuhrmann et al. 1999)

opencc-by-4.0Jun 2016View details →
zenodo28/100

Figure 1 from: Molino J, Lubiana Alves T, Ferreira-Camargo L, Croce M, Tanaka A, Buson F, Ribeiro P, Campos-Salazar A, Antonio E, Maizel A, Siratuti V, Costa C, Wlodarczyk S, de Souza Lima R, Mello F, Mayfield S, Carvalho J (2016) Chimeric spider silk production in microalgae: a modular bionanomaterial. Research Ideas and Outcomes 2: e9342. https://doi.org/10.3897/rio.2.e9342

Figure 1 - Project overview. Schematic representation of spider web structure from macro to nano scale. A representation of: enzybiotic protein from a bacteriophage; a spider silk protein with repetitive domains and N and C terminals; host expression system Chlamydomonas reinhardtii and a chimeric protein envisioned in this project; and the final product, a biopatch produced from recombinant silk proteins and chimeric proteins.

opencc-by-4.0Jun 2016View details →
zenodo28/100

Figure 2 from: Molino J, Lubiana Alves T, Ferreira-Camargo L, Croce M, Tanaka A, Buson F, Ribeiro P, Campos-Salazar A, Antonio E, Maizel A, Siratuti V, Costa C, Wlodarczyk S, de Souza Lima R, Mello F, Mayfield S, Carvalho J (2016) Chimeric spider silk production in microalgae: a modular bionanomaterial. Research Ideas and Outcomes 2: e9342. https://doi.org/10.3897/rio.2.e9342

Figure 2 - Schematic representation of spider silk proteins and chimeric protein. A: MaSp1 - Major ampullate spidroin 1, MaSp2 - Major ampullate spidroin 2 B: Chimeric protein of a enzybiotic with N and C terminals domains of spider silk proteins.

opencc-by-4.0Jun 2016View details →
zenodo28/100

Figure 4 from: Molino J, Lubiana Alves T, Ferreira-Camargo L, Croce M, Tanaka A, Buson F, Ribeiro P, Campos-Salazar A, Antonio E, Maizel A, Siratuti V, Costa C, Wlodarczyk S, de Souza Lima R, Mello F, Mayfield S, Carvalho J (2016) Chimeric spider silk production in microalgae: a modular bionanomaterial. Research Ideas and Outcomes 2: e9342. https://doi.org/10.3897/rio.2.e9342

Figure 4 - Experimental Flowchart. (A) Wild Cells incubated with built vectors. (B) Wild-cell transformation by electroporation. (C) Selection of mutants resistant to Zeocin. (D) Screening of antibiotic resistant cells by PCR. (E) Cultivation of PCR positive cells. (F) Fractions to be tested for the presence of recombinant proteins. (G) Detection of recombinant proteins present in the fractions by Western Blot. (H) Protein Purification. (I) Quantification via ELISA. (J) Spider silk polymerization reaction.

opencc-by-4.0Jun 2016View details →
geo24/100

Transcriptome changes reveal the toxic mechanism of cadmium and lead combined exposure on silk production and web-weaving behavior of spider A. ventricosus

GEO Series GSE240836. Araneus ventricosus. 24 samples. Type: Expression profiling by high throughput sequencing.

openGEO-OpenAug 2023View details →

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