Spider silk - Knowledge

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proteins form a soft micelle of several tens of nanometers by self-organization because the hydrophilic terminals are excluded. In ampullate, the concentration of the protein is high. Then, the micelles are squeezed into the duct. The long axis direction of the molecules is aligned parallel to the duct by a mechanical frictional force and partially oriented. The continuous lowering of pH from 7.5 to 8.0 in the tail to presumably close to 5.0 occurs at the end of the duct. Ion exchange, acidification, and water removal all happen in the duct. The shear and elongational forces lead to phase separation. In the acidic bath of the duct, the molecules attain a high concentration liquid crystal state. Finally, the silk is spun from the taper exterior. The molecules become more stable helixes and β-sheets from the liquid crystal.

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Sticky balls drawn in blue are made at equal intervals on the spiral line with viscous material secreted from the aggregate gland. Attachment cement secreted from the piriform gland is used to connect and fix different lines. Microscopically, the spider silk secondary structure is formed of spidroin with the structure shown on the right side. In the dragline and radial line, a crystalline β-sheet and an amorphous helical structure are interwoven. The large amount of β-spiral structure gives elastic properties to the capture part of the orb web. In the structural modules diagram, a microscopic structure of dragline and radial lines is shown, composed mainly of two proteins of MaSp1 and MaSp2, as shown in the upper central part. The spiral line has no crystalline β-sheet region.

43: 142: 3275: 2482: 820: 29: 691: 287: 886: 7329: 1038: 984:, an important factor in fibre formation. This section is lined with cells that exchange ions, reduce the dope pH from neutral to acidic, and remove water from the fibre. Collectively, the shear stress and the ion and pH changes induce the liquid silk dope to undergo a phase transition and condense into a solid protein fibre with high molecular organisation. The spigot at the end has lips that clamp around the fibre, controlling fibre diameter and further retaining water. 8076: 7530: 929: 957: 1811: 8086: 703: 177:) of the nanofibril. Glycine is mostly found in the so-called amorphous matrix consisting of helical and beta turn structures. The interplay between the hard crystalline segments and the strained elastic semi-amorphous regions gives spider silk its extraordinary properties. Various compounds other than protein are used to enhance the fibre's properties. 1286:

Recombinant spider silk proteins can self-assemble at the liquid-air interface of a standing solution to form protein-permeable, strong and flexible nanomembranes that support cell proliferation. Potential applications include skin transplants, and supportive membranes in organ-on-a-chip. These nanomembranes have been used to create a static

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Researchers from Japan's RIKEN Center constructed an artificial gland that reproduced spider silk's molecular structure. Precise microfluidic mechanisms directed proteins to self-assemble into functional fibers. The process used negative pressure to pull (rather than push) a spidroin solution through

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venture from shelter and leave a trail of silk, use that as an emergency line in case of falling from inverted or vertical surfaces. Others, even web dwellers, deliberately drop from a web when alarmed, using a silken thread as a drop line by which they can return in due course. Some, such as species

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The final length is the tapering duct, the site of most of the fibre formation. This consists of a tapering tube with several tight sharp turns, a valve near the end includes a spigot from which the solid silk fibre emerges. The tube tapers hyperbolically, therefore the unspun silk is under constant

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Silk can be formed into other shapes and sizes such as spherical capsules for drug delivery, cell scaffolds and wound healing, textiles, cosmetics, coatings, and many others. Spider silk proteins can self-assemble on superhydrophobic surfaces into nanowires, as well as micron-sized circular sheets.

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To artificially synthesise spider silk into fibres, two broad tasks are required. These are synthesis of the feedstock (the unspun silk dope in spiders), and synthesis of the production conditions (the funnel, valve, tapering duct, and spigot). Few strategies have produced silk that can efficiently

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bacteria, yeasts, plants, silkworms, and animals other than silkworms have been used to produce spider silk-like proteins, which have different characteristics than those from a spider. Extrusion of protein fibres in an aqueous environment is known as "wet-spinning". This process has produced silk

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The leftmost section s the secretory or tail section. The walls of this section are lined with cells that secrete proteins Spidroin I and Spidroin II, the main components of this spider's dragline. These proteins are found in the form of droplets that gradually elongate to form long channels along

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Schematic of the spider's orb web, structural modules, and spider silk structure. On the left is shown a schematic drawing of an orb web. The red lines represent the dragline, radial line, and frame lines. The blue lines represent the spiral line, and the centre of the orb web is called the "hub".

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is an old technique whereby a fluid is held in a container such that it flows out through capillary action. A conducting substrate is positioned below, and a difference in electrical potential is applied between the fluid and the substrate. The fluid is attracted to the substrate, and tiny fibres

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Schematic of the spiders spinning apparatus and structural hierarchy in silk assembling related to assembly into fibers. In the process of dragline production, the primary structure protein is secreted first from secretory granules in the tail. In the ampullate (neutral environment, pH = 7), the

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All spiders produce silks, and a single spider can produce up to seven different types of silk for different uses. This is in contrast to insect silks, where an individual usually only produces a single type. Spiders use silks in many ways, in accord with the silk's properties. As spiders have

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under ambient conditions, become functional immediately, and are usable indefinitely, remaining biodegradable, versatile and compatible with other materials in the environment. The adhesive and durability properties of the attachment disc are controlled by functions within the spinnerets. Some

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The molecular structure of unspun silk is both complex and long. Though this endows the fibres with desirable properties, it also complicates replication. Various organisms have been used as a basis for attempts to replicate necessary protein components. These proteins must then be extracted,

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fibres of diameters ranging from 10 to 60 μm, compared to diameters of 2.5–4 μm for natural spider silk. Artificial spider silks have fewer and simpler proteins than natural dragline silk, and consequently offer half the diameter, strength, and flexibility of natural dragline silk.

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Meeting the specification for all these ecological uses requires different types of silk presenting different properties, as either a fibre, a structure of fibres, or a globule. These types include glues and fibres. Some types of fibres are used for structural support, others for protective

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The spinning process occurs when a fibre is pulled away from the body of a spider, whether by the spider's legs, by the spider's falling under its own weight, or by any other method. The term "spinning" is misleading because no rotation occurs. It comes from analogy to the textile

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When exposed to water, dragline silks undergo supercontraction, shrinking up to 50% in length and behaving like a weak rubber under tension. Many hypotheses have attempted to explain its use in nature, most popularly to re-tension webs built in the night using the morning dew.

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Capturing lines. Sticky, stretchy, and tough. The capture spiral is sticky due to droplets of aggregate (a spider glue) that are placed on the spiral. The elasticity of flagelliform allows enough time for the aggregate to adhere to the aerial prey flying into the web.

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Arakawa, Kazuharu; Kono, Nobuaki; Malay, Ali D.; Tateishi, Ayaka; Ifuku, Nao; Masunaga, Hiroyasu; Sato, Ryota; Tsuchiya, Kousuke; Ohtoshi, Rintaro; Pedrazzoli, Daniel; Shinohara, Asaka; Ito, Yusuke; Nakamura, Hiroyuki; Tanikawa, Akio; Suzuki, Yuya (14 October 2022).

710: 1395:; the milk produced by the goats contained significant quantities of the protein, 1–2 grams of silk proteins per litre of milk. Attempts to spin the protein into a fibre similar to natural spider silk resulted in fibres with tenacities of 2–3 grams per 353:

Consisting of mainly protein, silks are about a sixth of the density of steel (1.3 g/cm). As a result, a strand long enough to circle the Earth would weigh about 2 kilograms (4.4 lb). (Spider dragline silk has a tensile strength of roughly

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The fibres' microstructural information and macroscopic mechanical properties are related. Ordered regions (i) mainly reorient by deformation for low-stretched fibres and (ii) the fraction of ordered regions increases progressively for higher fibre

941:. Depending on the complexity of the species, spiders have two to eight spinnerets, usually in pairs. Species have varying specialised glands, ranging from a sac with an opening at one end, to the complex, multiple-section ampullate glands of the 992:, regulating the thickness of the fibre, and/or clamping the fibre as a spider falls upon it. The similarity of the silk worm's silk press and the roles each of these valves play in the silk production in these two organisms are under discussion. 1224:

Although cheap and easy to produce, gland shape and conditions are loosely approximated. Fibres created using this method may need encouragement to solidify by removing water from the fibre with chemicals such as (environmentally undesirable)

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Lazaris, A.; Arcidiacono, S, S; Huang, Y, Y; Zhou, J. F., JF; Duguay, F, F; Chretien, N, N; Welsh, E. A., EA; Soares, J. W., JW; Karatzas, C. N., CN (2002). "Spider silk fibers spun from soluble recombinant silk produced in mammalian cells".

708: 358:. The tensile strength listed for steel might be slightly higher – e.g. 1.65 GPa, but spider silk is a much less dense material, so that a given weight of spider silk is five times as strong as the same weight of steel.) 5317:

Gustafsson L, Tasiopoulos CP, Jansson R, Kvick M, Duursma T, Gasser TC, Wijngaart W, Hedhammar M (2020), "Recombinant Spider Silk Forms Tough and Elastic Nanomembranes that are Protein-Permeable and Support Cell Attachment and Growth",

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Bolt Threads produced a recombinant spidroin using yeast, for use in apparel fibers and personal care. They produced the first commercial apparel products made of recombinant spider silk, trademarked Microsilk, demonstrated in ties and

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Arcidiacono, S.; Mello, Charlene M.; Butler, Michelle; Welsh, Elizabeth; Soares, Jason W.; Allen, Alfred; Ziegler, David; Laue, Thomas; Chase, Susan (2002). "Aqueous processing and fiber spinning of recombinant spider silks".

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is the resistance to deformation elastically along the tensile force direction. Unlike steel or Kevlar which are stiff, spider silk is ductile and elastic, having lower Young's modulus. According to Spider Silkome Database,

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have the advantage of being controllable and able to test spin small volumes of unspun fibre, but setup and development costs are high. A patent has been granted and continuously spun fibres have achieved commercial use.

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In some cases, spiders may use silk as a food source. While methods have been developed to collect silk from a spider by force, gathering silk from many spiders is more difficult than from silk-spinning organisms such as

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Silk production differs in an important aspect from that of most other fibrous biomaterials. It is pulled on demand from a precursor out of specialised glands, rather than continuously grown like plant cell walls.

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Lucas, F.; Shaw, J. T. B. & Smith, S. G. (1960). "Comparative studies of fibroins.I. The amino acid composition of various fibroins and its significance in relation to their crystal structure and taxonomy".

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targets during laser ignition, as it remains considerably elastic and has a high energy to break at temperatures as low as 10–20 K. In addition, it is made from "light" atomic number elements that emit no

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structures. Some can absorb energy effectively, whereas others transmit vibration efficiently. These silk types are produced in different glands; so the silk from a particular gland can be linked to its use.

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While unlikely to be relevant in nature, dragline silks can hold their strength below -40 °C (-40 °F) and up to 220 °C (428 °F). As occurs in many materials, spider silk fibres undergo a

2047: 1000:, arising in part due to the high protein concentration of silk dope (around 30% in terms of weight per volume). This allows the silk to flow through the duct as a liquid while maintaining molecular order. 987:

Almost at the end is a valve. Though discovered some time ago, its precise purpose is still under discussion. It is believed to assist in restarting and rejoining broken fibres, acting much in the way of a

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Seidel, A.; Liivak, Oskar; Calve, Sarah; Adaska, Jason; Ji, Gending; Yang, Zhitong; Grubb, David; Zax, David B.; Jelinski, Lynn W. (2000). "Regenerated spider silk: Processing, properties, and structure".

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Gustafsson, L.; Jansson, R.; Hedhammar, M. & van der Wijngaart, W. (2018). "Structuring of Functional Spider Silk Wires, Coatings, and Sheets by Self-Assembly on Superhydrophobic Pillar Surfaces".

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invented a reeling device for harvesting spider silk directly from spiders, allowing it to be spun into threads. Neither Bon nor Termeyer were successful in producing commercially viable quantities.

910:, similar to extrusion, with the subtlety that the force is induced by pulling at the finished fibre rather than squeezing it out of a reservoir. The fibre is pulled through (possibly multiple) silk 301:

The variability of spider silk fibre mechanical properties is related to their degree of molecular alignment. Mechanical properties also depend on ambient conditions, i.e. humidity and temperature.

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Gustafsson, L.; Jansson, R.; Hedhammar, M.; van der Wijngaart, W. (2018). "Structuring of Functional Spider Silk Wires, Coatings, and Sheets by Self-Assembly on Superhydrophobic Pillar Surfaces".

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and cover wounds with the inner lining. It reportedly facilitated healing, and connected with the skin. This is believed to be due to the silk's antiseptic properties, and because silk is rich in

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Lefèvre, T.; Boudreault, S.; Cloutier, C. & Pézolet, M. (2008). "Conformational and orientational transformation of silk proteins in the major ampullate gland of Nephila clavipes spiders".

1399:. Nexia used wet spinning and squeezed the silk protein solution through small extrusion holes to simulate the spinneret, but this was not sufficient to replicate native spider silk properties. 1162:

was engineered to produce a 556 kDa protein. Fibers spun from these synthetic spidroins are the first to fully replicate the mechanical performance of natural spider silk by all common metrics.

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Gustafsson, Linnea; Panagiotis Tasiopoulos, Christos; Jansson, Ronnie; Kvick, Mathias; Duursma, Thijs; Gasser, Thomas Christian; van der Wijngaart, Wouter; Hedhammar, My (16 August 2020).

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Lefvre, T.; Boudreault, S.; Cloutier, C.; Pezolet, M. (2008). "Conformational and orientational transformation of silk proteins in the major ampullate gland of Nephila clavipes spiders".

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Elices, M.; Guinea, G. V.; Plaza, G. R.; Karatzas, C.; Riekel, C.; Agulló-Rueda, F.; Daza, R.; Pérez-Rigueiro, J. (2011). "Bioinspired Fibers Follow the Track of Natural Spider Silk".

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used in optical communications. Silk has been used to create biolenses that could be used in conjunction with lasers to create high-resolution images of the inside of the human body.

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Some spiders that do not spin actual traps build alarm webs that the feet of their prey (such as ants) can disturb, cueing the spider to pounce on prey or flee a formidable intruder.

7043:; Taylor, T S; Black, A M; Davenport, W E; Varmette, P G (2011). "N-slit interferometer for secure free-space optical communications: 527 m intra interferometric path length". 128:. Observations of male spiders producing silk during sexual interactions are common across widespread taxa. The function of male-produced silk in mating has received little study. 1249:

Self-assembly of silk at standing liquid-gas interphases of a solution tough and strong sheets. These sheets are now explored for mimicking the basal membrane in tissue modeling.

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Elices, M.; Plaza, G.R.; Arnedo, M.A.; Perez-Rigueiro, J.; Torres, F.G. & Guinea, G. (2009). "Mechanical Behavior of Silk During the Evolution of Orb-Web Spinning Spiders".

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Zhao, Yue; Li, Yanrong; Hien, K. T. T.; Mizutani, Goro; Rutt, Harvey N. (2019). "Observation of Spider Silk by Femtosecond Pulse Laser Second Harmonic Generation Microscopy".

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Sapede, D.; Seydel, T.; Forsyth, V. T.; Koza, M. M.; Schweins, R.; Vollrath, F.; Riekel, C. (2005). "Nanofibrillar structure and molecular mobility in spider dragline silk".

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Sponner, A.; Vater, Wolfram, Wolfram; Monajembashi, Shamci, Shamci; Unger, Eberhard, Eberhard; Grosse, Frank, Frank; Weisshart, Klaus, Klaus (2007). Scheibel, Thomas (ed.).

614:). Threads radiate out of the nest to provide a sensory link to the outside. Silk is a component of the lids of spiders that use "trapdoors", such as members of the family 2677:

Plaza, Gustavo R.; Guinea, Gustavo V.; Pérez-Rigueiro, José; Elices, Manuel (2006). "Thermo-hygro-mechanical behavior of spider dragline silk: Glassy and rubbery states".

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Guinea, G.V.; Elices, M.; Pérez-Rigueiro, J. & Plaza, G.R. (2005). "Stretching of supercontracted fibers: a link between spinning and the variability of spider silk".

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Arcidiacono, S.; Mello, C.; Kaplan, D.; Cheley, S. & Bayley, H. (1998). "Purification and characterization of recombinant spider silk expressed in Escherichia coli".

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Simmons, A.; Ray, E. & Jelinski, L. W. (1994). "Solid-State C-13 NMR of Nephila-Clavipes Dragline Silk Establishes Structure and Identity of Crystalline Regions".

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The ampulla (storage sac) is next. This stores and maintains the gel-like unspun silk dope. In addition, it secretes proteins that coat the surface of the final fibre.

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Simmons, A. H.; Michal, C. A. & Jelinski, L. W. (1996). "Molecular orientation and two-component nature of the crystalline fraction of spider dragline silk".

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Gustafsson, L.; Kvick, M.; Åstrand, C.; Ponsteen, N.; Dorka, N.; Hegrová, V.; Svanberg, S.; Horák, J.; Jansson, R.; Hedhammar, M.; van der Wijngaart, W. (2023).

224:. Refinements to this model include: semi-crystalline regions were found as well as a fibrillar skin core model suggested for spider silk, later visualised by 1831: 4753: 6346:

Shao, Z.; Vollrath, F.; Sirichaisit, J. & Young, R. J. (1999). "Analysis of spider silk in native and supercontracted states using Raman spectroscopy".

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evolved, so has their silks' complexity and uses, for example from primitive tube webs 300–400 million years ago to complex orb webs 110 million years ago.

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Dicko, C.; Porter, D.; Bond, J.; Kenney, J. M. & Vollratht, F. (2008). "Structural disorder in silk proteins reveals the emergence of elastomericity".

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eats the silk of host spider webs. Some daily weavers of temporary webs eat their own unused silk, thus mitigating an otherwise heavy metabolic expense.

124:. Silk produced by females provides a transmission channel for male vibratory courtship signals, while webs and draglines provide a substrate for female 6408:

Knight, D. P.; Knight, M. M. & Vollrath, F. (2000). "Beta transition and stress-induced phase separation in the spinning of spider dragline silk".

4704: 2532:"Relationship between microstructure and mechanical properties in spider silk fibers: identification of two regimes in the microstructural changes" 2294:

Papadopoulos, P.; Ene, R.; Weidner, I.; Kremer, F. (2009). "Similarities in the Structural Organization of Major and Minor Ampullate Spider Silk".

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Blackledge, TA; Hayashi, CY (2006). "Silken toolkits: Biomechanics of silk fibers spun by the orb web spider Argiope argentata (Fabricius 1775)".

1277:, to the substrate, drying as they travel. This method creates nano-scale fibres from silk dissected from organisms and regenerated silk fibroin. 3176:

Yang, Y.; Chen, X.; Shao, Z.; Zhou, P.; Porter, D.; Knight, D. P.; Vollrath, F. (2005). "Toughness of Spider Silk at High and Low Temperatures".

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Magoshi, J.; Magoshi, Y. & Nakamura, S. (1985). "Physical properties and structure of silk: 9. Liquid crystal formation of silk fibroin".

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Some wandering spiders leave a largely continuous trail of silk impregnated with pheromones that the opposite sex can follow to find a mate.

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who, using a process similar to creating silkworm silk, wove silk derived spider's egg cocoons into stockings and gloves. Fifty years later

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Riekel, C. & Vollrath, F. (2001). "Spider silk fibre extrusion: combined wide- and small-angle X- ray microdiffraction experiments".

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Zhao, Yue; Hien, Khuat Thi Thu; Mizutani, Goro; Rutt, Harvey N. (June 2017). "Second-order nonlinear optical microscopy of spider silk".

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Replicating the complex conditions required to produce comparable fibres has challenged research and early-stage manufacturing. Through

534:(typical orb-weavers); tube webs; tangle webs; sheet webs; lace webs, dome webs; single thread used by the Bolas spiders for "fishing". 6373:

Riekel, C.; Bränden, C; Craig, C; Ferrero, C; Heidelbach, F; Müller, M (1999). "Aspects of X-ray diffraction on single spider fibers".

406:(aromatic nylon) filaments, which themselves are benchmarks of modern polymer fibre technology". According to Spider Silkome Database, 7179: 1298: 3049:

Porter, D.; Vollrath, F.; Shao, Z. (2005). "Predicting the mechanical properties of spider silk as a model nanostructured polymer".

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Spiber produced a synthetic spider silk (Q/QMONOS). In partnership with Goldwin, a ski parka made from this was in testing in 2016.

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Jackson, Robert R. (1974). "Effects of D-Amphetamine Sulfate and Diazepam on Thread Connection Fine Structure in a Spider's Web".

5613:"Recombinant Spider Silk Forms Tough and Elastic Nanomembranes that are Protein-Permeable and Support Cell Attachment and Growth" 1213:

Spider silks with comparatively simple molecular structure need complex ducts to be able to form an effective fibre. Approaches:

7087: 1823: 5160:"Native-sized recombinant spider silk protein produced in metabolically engineered Escherichia coli results in a strong fiber" 4969:, Lewis, R. V., "Expression of spider silk proteins", published 2010-05-25, assigned to University of Wyoming 1241:

Placing a solution of spider silk on a superhydrophobic surface can generate sheets, particles, and nanowires of spider silk.

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Plaza, G.R.; Pérez-Rigueiro, J.; Riekel, C.; Perea, G.B.; Agulló-Rueda, F.; Burghammer, M.; Guinea, G.V.; Elices, M. (2012).

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Osaki, Shigeyoshi (2012). "Spider Silk Violin Strings with a Unique Packing Structure Generate a Soft and Profound Timbre".

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Kluge, Jonathan A.; Rabotyagova, Olena; Leisk, Gary G.; Kaplan, David L. (May 2008). "Spider silks and their applications".

7268: 5646:"Fibrillar Nanomembranes of Recombinant Spider Silk Protein Support Cell Co-culture in an in Vitro Blood Vessel Wall Model" 5356:"Fibrillar Nanomembranes of Recombinant Spider Silk Protein Support Cell Co-culture in an In Vitro Blood Vessel Wall Model" 4507:

Vollrath, F. & Knight, D. P. (1998). "Structure and function of the silk production pathway in spider Nephila edulis".

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Combined effect of humidity and temperature on mechanical properties. Glass-transition temperature dependence on humidity.

1009:(garden cross spider) consists of many glands shown below. A similar gland architecture appears in the black widow spider. 267:

Most silks, in particular dragline silk, have exceptional mechanical properties. They exhibit a unique combination of high

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Vollrath, F. & Edmonds, D. T. (1989). "Modulation of the Mechanical-Properties of Spider Silk By Coating With Water".

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Wen, H. X.; et al. (2010). "Transgenic silkworms (Bombyx mori) produce recombinant spider dragline silk in cocoons".

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Knight, D. P.; Vollrath, F. (1 April 2001). "Changes in element composition along the spinning duct in a Nephila spider".

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Chen, Xin; Knight, David P.; Vollrath, Fritz (1 July 2002). "Rheological characterization of nephila spidroin solution".

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Many species have different glands to produce silk with different properties for different purposes, including housing,

105:, or to glide away from predators. Most spiders vary the thickness and adhesiveness of their silk according to its use. 8115: 6605: 6266: 4166:"Carbonic anhydrase generates CO2 and H+ that drive spider silk formation via opposite effects on the terminal domains" 2386: 42: 2098:"Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber" 1550:"Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber" 948:

Behind each spinneret on the surface of the spider lies a gland, a generalised form of which is shown in the figure.

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Strength and toughness are distinct quantities. Weight for weight, silk is stronger than steel, but not as strong as

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properties that keep the silk moist while warding off ant invasion. It occurs in high concentration in glue threads.

7566: 7370: 3531: 1977:"Silk feeding as an alternative foraging tactic in a kleptoparasitic spider under seasonally changing environments" 1194:

Genetically modified to produce silk proteins. Patents were granted in 2010, but no fibres have yet been described.

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Elongation at break compares initial object length to final length at break. According to Spider Silkome Database,

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Bowen, C.H. (2018). "Recombinant Spidroins Fully Replicate Primary Mechanical Properties of Natural Spider Silk".

4217:"Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation" 1563:"Solid-State C-13 Nmr of Nephila-Clavipes Dragline Silk Establishes Structure and Identity of Crystalline Regions" 484:

secretion, spun into patterns (called "attachment discs") using a minimum of silk substrate. The pyriform threads

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Sutherland, TD; Young, JH; Weisman, S; Hayashi, CY; Merritt, DJ (2010). "Insect silk: One name, many materials".

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Kerkam, K.; Viney, C.; Kaplan, D. & Lombardi, S. (1991). "Liquid Crystallinity of Natural Silk Secretions".

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Tasiopoulos, Christos Panagiotis; Gustafsson, Linnea; van der Wijngaart, Wouter; Hedhammar, My (25 June 2021).

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Vollrath, F.; Holtet, T.; Thogersen, H. C. & Frische, S. (1996). "Structural organization of spider silk".

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The web's outer rim and spokes and the lifeline. Can be as strong per unit weight as steel, but much tougher.

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Each spider and each type of silk has a set of mechanical properties optimised for their biological function.

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Dragline silk – used for the web's outer rim and spokes, also for lifeline and for ballooning

5703: 3224:"Bioprospecting Finds the Toughest Biological Material: Extraordinary Silk from a Giant Riverine Orb Spider" 2019:

Work, Robert W.; Emerson, Paul D. (1982). "An Apparatus and Technique for the Forcible Silking of Spiders".

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The funnel rapidly reduces the large diameter of the storage sac to the small diameter of the tapering duct.

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Heim, M.; Keerl, D. & Scheibel, T. (2009). "Spider Silk: From Soluble Protein to Extraordinary Fiber".

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Kluge, J. A.; Rabotyagova, O.; Leisk, G. G.; Kaplan, D. L. (2008). "Spider silks and their applications".

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during irradiation that could preheat the target, limiting the pressure differential required for fusion.

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First important paper suggesting the water interplay with spider silk fibroin modulating silk properties.

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silk is more than twice as tough as any previously described silk and over 10 times tougher than Kevlar".

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Xia, Xiao-Xia; Qian, Zhi-Gang; Ki, Chang Seok; Park, Young Hwan; Kaplan, David L.; Lee, Sang Yup (2010).

4966: 1947: 1370: 232:. Sizes of the nanofibrillar structure and the crystalline and semi-crystalline regions were revealed by 93:

traps to catch prey, to entangle and restrain prey before biting, to transmit tactile information, or as

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Gosline, J. M.; DeMont, M. E. & Denny, M. W. (1986). "The structure and properties of spider silk".

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Jeffery, F; La Mattina, C; Tuton-Blasingame, T; Hsia, Y; Gnesa, E; Zhao, L; Franz, A; Vierra, C (2011).

3295:"Spider's super-glue: Thread anchors are composite adhesives with synergistic hierarchical organization" 317:

silk has the highest Young's modulus with 37 GPa, compared to 208 GPa for steel and 112 GPa for Kevlar.

8110: 6643: 2786: 5847:"University of Notre Dame and Kraig Biocraft Laboratories Create Artificial Spider Silk Breakthrough" 5509: 1888:

and extract silk from them. In 2012, spider silk fibres were used to create a set of violin strings.

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First time mechanical properties of spider silk compared with other materials in a scientific paper.

3274: 2481: 1996: 1677:"Molecular orientation and two-component nature of the crystalline fraction of spider dragline silk" 1666:

X-ray evidence presented in this paper; simple model of crystallites embedded in amorphous regions.

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the length of the final fibre, hypothesised to assist in preventing crack formation or self-healing.

7318: 7261: 5880: 5799:[Wire strength: spin doctors make super strong fake cobweb] (in Dutch). KIJK. 21 April 2012 1378: 173:. On a secondary level, the short side-chained alanine is mainly found in the crystalline domains ( 47: 6954:

Allmeling, Christina; Jokuszies, Andreas; Reimers, Kerstin; Kall, Susanne; Vogt, Peter M. (2006).

6646:(1995). "Construction, Cloning, and Expression of Synthetic Genes Encoding Spider Dragline Silk". 6088:

Lucas, F.; Shaw, J. T. B. & Smith, S. G. (1960). "The Composition of Arthropod Silk Fibrons".

2200:"The molecular structure of spider dragline silk: Folding and orientation of the protein backbone" 1748:"Stretching of supercontracted fibers: a link between spinning and the variability of spider silk" 1633:"The molecular structure of spider dragline silk: Folding and orientation of the protein backbone" 1345:

dragline spidroin, having similar mechanical characteristics as their natural counterparts, i.e.,

52: 8130: 8089: 7198: 6956:"Use of spider silk fibres as an innovative material in a biocompatible artificial nerve conduit" 4985:

Scheller, J. & Conrad, U. (2005). "Plant-based material, protein and biodegradable plastic".

2257:

Liu, Y.; Sponner, A.; Porter, D.; Vollrath, F. (2008). "Proline and Processing of Spider Silks".

2048:"A review of the mechanisms and functional roles of male silk use in spider courtship and mating" 1619:"Spider silk fibre extrusion: combined wide- and small-angle X- ray microdiffraction experiments" 1073: 698:

immobilizing prey by wrapping a curtain of aciniform silk around the insect for later consumption

638:

Some spiders that venture from shelter leave a silk trail by which to find their way home again.

457: 225: 56: 5945:"Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins" 4705:"Spider dragline silk: Correlated and mosaic evolution in high-performance biological materials" 4410:

Heinhorst, S.; Cannon, G. (2002). "Nature: Self-Healing Polymers and Other Improved Materials".

3566:

Cunningham, Aimee (2009). "Taken for a spin: Scientists look to spiders for the goods on silk".

3407: 2826:"Kevlar-based Composite Material and its Applications in Body Armour: A Short Literature Review" 5884: 3556:

Holm, Erik, Dippenaar-Schoeman, Ansie; Goggo Guide; LAPA publishers (URL: WWW.LAPA.co.za). 2010

1991: 961: 942: 890: 719: 20: 5994: 1302:

Proposed framework for producing artificial skin from spider silk to help patients with burns.

5854: 4747: 2824:

Nair, Anand Narayanan; Sundharesan, Santhosh; Al Tubi, Issa Saif Mohammed (1 November 2020).

1940: 1605:"Beta transition and stress-induced phase separation in the spinning of spider dragline silk" 1447:"Eine Analyse der Gespinste der Kreuzspinne" (Amino acid composition analysis of spider silk) 1374: 997: 2841: 2428: 1872:. However, due to the difficulties in extracting and processing, the largest known piece of 1783:"Purification and characterization of recombinant spider silk expressed in Escherichia coli" 996:

Throughout the process the silk appears to have a nematic texture, in a manner similar to a

7917: 7879: 7559: 7308: 7052: 6880: 6733: 6724:

Seidel, A.; Liivak, O. & Jelinski, L. W. (1998). "Artificial Spinning of Spider Silk".

6565: 6514: 6320: 6226: 6152: 5742: 5569: 5559: 5464: 5226: 5216: 5171: 5132: 5096: 5041: 4994: 4932: 4780: 4702: 4454: 4419: 4228: 4050: 3957: 3355: 3344:"Cobweb-weaving spiders produce different attachment discs for locomotion and prey capture" 3306: 3235: 3185: 3112: 3058: 3000: 2882: 2837: 2733: 2686: 2588: 2543: 2504: 2442: 2395: 2358: 2211: 2153: 1897: 610: 141: 6853: 6010:"Synthetic spider silk could be the biggest technological advance in clothing since nylon" 866:

Wrap and secure prey. Two to three times as tough as the other silks, including dragline.

8: 8120: 7892: 7775: 7293: 7254: 6641: 5404:"Tunable Silk: Using Microfluidics to Fabricate Silk Fibers with Controllable Properties" 3222:

Agnarsson, Ingi; Kuntner, Matjaž; Blackledge, Todd A. (2010). Lalueza-Fox, Carles (ed.).

2850: 2825: 1307: 813: 724: 620: 576: 102: 7064: 7056: 6884: 6737: 6569: 6518: 6505:

Vollrath, F. & Porter, D. (2006). "Spider silk as an archetypal protein elastomer".

6324: 6230: 6156: 5746: 5573: 5468: 5230: 5175: 5136: 5100: 5045: 4998: 4936: 4784: 4458: 4423: 4232: 4054: 3961: 3359: 3310: 3239: 3189: 3116: 3062: 3004: 2886: 2737: 2690: 2592: 2547: 2508: 2446: 2399: 2362: 2215: 2157: 1765:"Construction, Cloning, and Expression of Synthetic Genes Encoding Spider Dragline Silk" 819: 101:

to protect their offspring. They can use the silk to suspend themselves from height, to

7303: 7161: 7134: 7068: 6980: 6971: 6955: 6936: 6809: 6706: 6627: 6600: 6581: 6538: 6288: 6261: 6242: 5773: 5760: 5726: 5672: 5645: 5593: 5487: 5452: 5428: 5403: 5380: 5337: 5299: 5250: 5194: 5159: 5065: 4948: 4905: 4849: 4806: 4735: 4645: 4624: 4486: 4290: 4265: 4192: 4165: 4071: 4038: 3981: 3922: 3897: 3845: 3753: 3735: 3667: 3640: 3618: 3444: 3400: 3258: 3223: 3201: 3136: 3103:

Vollrath, F. & Knight, D. P. (2001). "Liquid crystalline spinning of spider silk".

3082: 3026: 2898: 2762: 2721: 2652: 2604: 2578: 2465: 2430: 2411: 2177: 2075: 2028: 1848:

spider silk led to the manufacturing of military, medical, and consumer goods, such as

1577:"Analysis of spider silk in native and supercontracted states using Raman spectroscopy" 1005: 938: 549: 465: 309: 233: 190: 34: 6456: 6421: 6386: 6359: 6117: 5971: 5944: 5542: 5525: 4520: 4062: 3881: 3864: 2234: 2199: 2114: 2097: 1233:, and also may require later stretching of the fibre to achieve desirable properties. 7887: 7856: 7677: 7166: 6985: 6896: 6801: 6698: 6663: 6530: 6491: 6460: 6425: 6390: 6293: 6180: 6175: 6140: 6121: 6070: 5976: 5925: 5908: 5778: 5677: 5597: 5585: 5492: 5433: 5385: 5355: 5341: 5303: 5291: 5254: 5242: 5199: 5057: 5010: 4897: 4841: 4798: 4727: 4685: 4650: 4605: 4597: 4524: 4478: 4470: 4392: 4357: 4322: 4246: 4197: 4146: 4111: 4076: 4019: 3985: 3973: 3927: 3837: 3791: 3757: 3672: 3610: 3509: 3476: 3448: 3411: 3373: 3324: 3263: 3205: 3140: 3128: 3074: 3018: 2902: 2855: 2806: 2802: 2767: 2749: 2644: 2470: 2415: 2312: 2276: 2259: 2239: 2169: 2119: 2067: 1885: 1815: 1533:"Thermo-hygro-mechanical behavior of spider dragline silk: Glassy and rubbery states" 1406:

the device. The resulting fibers matched the hierarchical structure of natural fiber.

531: 422:

silk has the highest strain at break for any spider silk, breaking at 65% extension.

210: 150: 117: 6827: 6710: 6542: 6053:

Fischer, F. & Brander, J. (1960). "Eine Analyse der Gespinste der Kreuzspinne".

5662: 5371: 4952: 4909: 4853: 4739: 4490: 3849: 3622: 3529:

Flying spiders over Texas! Coast to Coast. Chad B., Texas State University Undergrad

3086: 2608: 2181: 2079: 1353:(13.7 ± 3.0 GPa), extensibility (18 ± 6%), and toughness (114 ± 51 MJ/m3). 390:, with some able to stretch up to five times their relaxed length without breaking. 28: 7533: 7156: 7146: 7072: 7060: 6975: 6967: 6892: 6888: 6791: 6741: 6690: 6655: 6622: 6614: 6585: 6573: 6522: 6487: 6452: 6417: 6382: 6355: 6328: 6283: 6275: 6246: 6234: 6170: 6160: 6113: 6062: 5966: 5956: 5917: 5796: 5768: 5750: 5727:"Native-sized recombinant spider silk protein produced in metabolically engineered 5667: 5657: 5624: 5577: 5537: 5482: 5472: 5423: 5415: 5375: 5367: 5327: 5281: 5234: 5189: 5179: 5140: 5104: 5069: 5049: 5002: 4940: 4887: 4879: 4833: 4810: 4788: 4719: 4677: 4667: 4640: 4632: 4589: 4516: 4462: 4427: 4384: 4349: 4314: 4285: 4277: 4236: 4187: 4177: 4138: 4103: 4066: 4058: 4037:

Hijirida, D. H.; Do, K. G.; Michal, C.; Wong, S.; Zax, D.; Jelinski, L. W. (1996).

4011: 3965: 3917: 3909: 3876: 3827: 3783: 3745: 3706: 3662: 3652: 3602: 3575: 3501: 3440: 3363: 3314: 3253: 3243: 3193: 3120: 3066: 3030: 3008: 2890: 2845: 2798: 2757: 2741: 2694: 2656: 2636: 2624: 2596: 2551: 2512: 2460: 2450: 2403: 2366: 2304: 2268: 2229: 2219: 2161: 2109: 2059: 2001: 1936: 1912: 1849: 1827: 1396: 1346: 1334: 1155: 1148: 690: 432: 326: 286: 268: 5921: 5832: 4015: 3948:

Vollrath, F.; Knight, D. P. (2001). "Liquid crystalline spinning of spider silk".

3816:"The role of terminal domains during storage and assembly of spider silk proteins" 3154: 2529: 2046:

Scott, Catherine E.; Anderson, Alissa G.; Andrade, Maydianne C. B. (August 2018).

116:

All spiders produce silk, although some spiders do not make webs. Silk is tied to

8079: 7902: 7864: 7657: 7552: 7494: 7463: 7337: 7313: 7298: 7151: 4182: 3913: 3579: 3535: 3505: 3248: 3070: 2965: 2455: 2383: 1845: 1350: 1269: 885: 275:). This enables a silk fibre to absorb a large amount of energy before breaking ( 7810: 6262:"The effect of spinning conditions on the mechanics of a spider's dragline silk" 6066: 5450: 4339: 2165: 1520:"The effect of spinning conditions on the mechanics of a spider's dragline silk" 1037: 544:"Swathing bands" to envelop prey. Often combined with immobilising prey using a 7950: 7755: 7610: 7515: 7380: 6780:"Sticky Layers and Shimmering Weaves: A Study of Two Human Uses of Spider Silk" 6345: 6145:

Proceedings of the National Academy of Sciences of the United States of America

5818: 5643: 5457:

Proceedings of the National Academy of Sciences of the United States of America

5353: 5164:

Proceedings of the National Academy of Sciences of the United States of America

4922: 4883: 4703:

Swanson, B. O.; Blackledge, T. A.; Summers, A. P. & Hayashi, C. Y. (2006).

4542:

Wilson, R. S. (1962). "The Control of Dragline Spinning in the Garden Spider".

3496:

Nentwig, Wolfgang; Heimer, Stefan (1987). "Ecological Aspects of Spider Webs".

2197: 1857: 1003:

As an example of a complex spinning field, the spinneret apparatus of an adult

964:. Each differently coloured section highlights a discrete section of the gland. 923: 903: 590: 367: 7208: 5267: 5006: 4837: 2600: 2005: 1822:

The earliest recorded attempt to weave fabric from spider silk was in 1709 by

1506:"Modulation of the Mechanical Properties of Spider Silk by Coating with Water" 579:

used by smaller spiders to float through the air, for instance for dispersal.

566:

Male spiders may produce sperm webs; spider eggs are covered in silk cocoons.

145:

Spider silk structure: crystalline beta-sheets separated by amorphous linkages

8125: 8104: 7968: 7940: 7927: 7825: 7740: 7583: 7479: 7403: 7388: 7360: 7355: 7345: 6805: 4601: 4474: 2859: 2810: 2753: 2071: 1884:

in 2009. Eighty-two people worked for four years to collect over one million

1877: 1853: 1460:"The Composition of Arthropod Silk Fibroins; Comparative studies of fibroins" 1385: 1341:

A 556 kDa spider silk protein was manufactured from 192 repeat motifs of the

1257: 1019:

300 aciniform glands for the outer lining of egg sacs, and for ensnaring prey

766:

Capture-spiral silk – used for the capturing lines of the web

355: 221: 125: 98: 7960: 6680: 6165: 5755: 5610: 5477: 5184: 5053: 5030: 4892: 3774:

Rising, A.; Johansson, J. (2015). "Toward spinning artificial spider silk".

2293: 1939:. In 2011, silk fibres were used to generate fine diffraction patterns over 1041:

Single strand of artificial spider silk produced under laboratory conditions

782:

Used to wrap and secure prey; used in male sperm webs; used in stabilimenta

722:. Repeated at variable slow motion to better see silk line. Spider probably 608:

Tube webs used by "primitive" spiders such as the European tube web spider (

481: 290:

An illustration of the differences between toughness, stiffness and strength

8025: 8015: 7945: 7720: 7712: 7170: 7040: 6989: 6900: 6618: 6534: 6464: 6429: 6394: 6297: 6279: 6125: 6074: 5980: 5961: 5929: 5782: 5681: 5629: 5612: 5589: 5581: 5496: 5437: 5389: 5332: 5295: 5286: 5269: 5246: 5238: 5203: 5061: 5014: 4901: 4845: 4802: 4731: 4689: 4654: 4609: 4528: 4482: 4396: 4388: 4361: 4326: 4281: 4250: 4201: 4150: 4115: 4023: 3977: 3931: 3841: 3795: 3676: 3614: 3452: 3377: 3328: 3267: 3197: 3132: 3078: 3022: 2771: 2745: 2648: 2474: 2407: 2316: 2308: 2280: 2243: 2224: 2063: 1694:

New insight and model to spider silk based on Group Interaction Modelling.

989: 981: 494: 6702: 6694: 6667: 6184: 4466: 4080: 3898:"Structure–function–property–design interplay in biopolymers: Spider silk" 3787: 3711: 3694: 2873:

Griffiths, J. R.; Salanitri, V. R. (1980). "The strength of spider silk".

2785:

Chen, Zhong; Gandhi, Umesh; Lee, Jinwoo; Wagoner, R. H. (1 January 2016).

2173: 2143: 2123: 1876:

made of spider silk is an 11-by-4-foot (3.4 by 1.2 m) textile with a

7935: 7785: 7725: 7682: 7615: 7489: 7443: 7433: 7398: 7285: 6796: 6779: 6555: 3896:

Tokareva, O.; Jacobsen, M.; Buehler, M.; Wong, J.; Kaplan, D. L. (2014).

3657: 1274: 1127: 715: 625: 436: 217: 216:

Termonia introduced this first basic model of silk in 1994. He suggested

213:

is believed to prevent the protein from denaturing in the acidic milieu.

178: 110: 7006:, The Sciences, The New York Academy of Sciences, September/October 1995 6813: 6659: 6601:"Liquid crystals and flow elongation in a spider's silk production line" 6332: 5764: 4304: 4266:"Liquid crystals and flow elongation in a spider's silk production line" 4129:

Lewis, R. V. (2006). "Spider silk: Ancient ideas for new biomaterials".

3528: 2370: 2256: 1721:"Liquid crystals and flow elongation in a spider's silk production line" 816:, or for a strand allowing the spider to drop down as silk is extruded). 8005: 8000: 7869: 7735: 7702: 7667: 7592: 7510: 7413: 7408: 7350: 6940: 6477: 5706:. Science Magazine, American Association for the Advancement of Science 5453:"Assembly mechanism of recombinant spider silk proteins (microfluidic)" 5354:

Tasiopoulos CP, Gustafsson L, Wijngaart W, van der Hedhammar M (2021),

4241: 4216: 3368: 3343: 3319: 3294: 2894: 2698: 2555: 2032: 1881: 1389: 928: 907: 805: 649: 615: 553: 403: 182: 174: 154: 86: 7907: 7847: 6745: 6407: 5419: 5144: 5108: 4944: 4681: 4593: 4353: 4318: 4142: 4107: 3832: 3815: 3606: 2640: 2516: 2272: 435:. The glass-transition temperature depends on humidity, as water is a 398:

The combination of strength and ductility gives dragline silks a high

8020: 7815: 7750: 7458: 7418: 7393: 6577: 6526: 6238: 6029:"Artificial spider gland spins scalable spider silk just like nature" 5270:"Scalable Production of Monodisperse Bioactive Spider Silk Nanowires" 4723: 4622: 4431: 3969: 3749: 3124: 2722:"1000 spider silkomes: Linking sequences to silk physical properties" 2349:

Termonia, Y. (1994). "Molecular Modeling of Spider Silk Elasticity".

1932: 1907: 1869: 594: 399: 276: 272: 170: 5451:

Rammensee, S.; Slotta, U.; Scheibel, T. & Bausch, A. R. (2008).

4793: 4768: 3013: 2988: 1134:

Silkworms genetically altered to express spider proteins and fibres.

7988: 7833: 7765: 7448: 7438: 6723: 6102: 6087: 3740: 3293:

Wolff, J. O.; Grawe, I; Wirth, M; Karstedt, A; Gorb, S. N. (2015).

2583: 2531: 2198:

van Beek, J. D.; Hess, S.; Vollrath, F. & Meier, B. H. (2002).

1861: 1810: 1360: 1226: 956: 280: 206: 158: 90: 7600: 4560: 1095:

silk is more than twice as tough as any previously described silk"

8047: 8042: 8037: 7897: 7605: 7428: 7423: 6310: 6259: 5316: 4636: 1865: 1230: 485: 387: 166: 162: 71: 7672: 7228:"Synthetic spider silk stronger and tougher than the real thing" 7039: 5523: 63:) depicts a peasant woman with a thread of gossamer in her hand. 8052: 7983: 7978: 7973: 7795: 7780: 7770: 7745: 7730: 7692: 7625: 7277: 5121: 4093: 3341: 2676: 1920: 1917: 1902: 1652:

First attempt to link structure with properties of spider silk

1476:"Structure of a Protein Superfiber − Spider Dragline Silk" 1381:

to create silkworms genetically altered to produce spider silk.

1356: 1055:

purified, and then spun before their properties can be tested.

338: 334: 295: 121: 82: 60: 7180:"The Tangled Web of Turning Spider Silk into a Super Material" 3342:

Sahni, V; Harris, J; Blackledge, T. A.; Dhinojwala, A (2012).

1975:

Miyashita, Tadashi; Maezono, Yasunori; Shimazaki, Aya (2004).

1745:

Guinea, G.V., Elices, M., Pérez-Rigueiro, J. & Plaza, G.R.

1608:

Secondary structural transition confirmation during spinning.

1530:

Plaza, G.R., Guinea, G.V., Pérez-Rigueiro, J. & Elices, M.

19:"Arachnidium" redirects here. For the genus of bryozoans, see 8057: 8010: 7993: 7912: 7697: 7687: 7662: 7640: 7630: 7575: 6953: 6372: 4625:"Microdissection of Black Widow Spider Silk-producing Glands" 4374: 3430: 1952: 1873: 1756:

Reconstituted /Synthetic Spider Silk and Artificial Spinning

1221:

Feedstock is forced through a hollow needle using a syringe.

911: 545: 498: 330: 202: 74: 7088:"Spider silk used to create lenses for imaging human tissue" 2431:"Composition and hierarchical organization of a spider silk" 1935:

in optical instruments such as telescopes, microscopes, and

1799:

First controlled wet-spinning of reconstituted spider silk.

1680:

Two types of alanine-rich crystalline regions were defined.

1178:

Genetically modified to secrete silk proteins in their milk.

341:

or Kevlar (3000 MPa). According to Spider Silkome Database,

7805: 7790: 7760: 7652: 7647: 7635: 7620: 5905: 5085: 4001: 3895: 2494: 1392: 812:, egg protection, and mobility (fine "gossamer" thread for 809: 490: 198: 94: 78: 7246: 7206: 6216: 6141:"Structure of a Protein Superfiber – Spider Dragline Silk" 3541: 3221: 1091:

Malagasy spider famed for making 25 m long strands. "

456:

The toughest known spider silk is produced by the species

7544: 7018:

Example of use of spider silk for telescopic rifle sights

6598: 4506: 3552: 3550: 3548: 3546: 3544: 3102: 2095: 1974: 1751:

Explanation of the variability of mechanical properties.

464:): "The toughness of forcibly silked fibers averages 350 5877:"Fraser Research Publicly Announced at Press Conference" 4039:"13C NMR of Nephila clavipes major ampullate silk gland" 3638: 2830:

IOP Conference Series: Materials Science and Engineering

2718: 1158:) is complex, but required for the strongest silk. Here 402:(or work to fracture), which "equals that of commercial 6642:

Prince, J. T.; McGrath, K. P.; Digirolamo, C. M. &

4766: 4409: 3943: 3941: 3538:

Describes the mechanical kiting of Spider "ballooning".

3292: 2787:"Variation and consistency of Young's modulus in steel" 758:

Used for temporary scaffolding during web construction

194: 6504: 6442: 6052: 4984: 3809: 3807: 3805: 2823: 1591:"Aspects of X-ray diffraction on single spider fibers" 1338:. This approach eliminates the need to "milk" spiders. 552:

the silk is combined with venom and squirted from the

169:

blocks, which is why silks are often referred to as a

3769: 3767: 3406:. Oxford; New York: Oxford University Press. p. 937:

The gland's visible, or external, part is termed the

798:

Bonds between separate threads for attachment point.

6055:

Hoppe-Seyler's Zeitschrift für Physiologische Chemie

4036: 3997: 3995: 3938: 3862: 3813: 2784: 2568: 2045: 1326:

Korea Advanced Institute of Science & Technology

6854:"1 Million Spiders Make Golden Silk for Rare Cloth" 6260:Vollrath, F.; Madsen, B. & Shao, Z. Z. (2001). 3802: 1154:Synthesising a large and repetitive molecule (~300 774:Egg cocoon silk – used for egg sacs 6138: 5797:"Draadkracht: spindoctors maken supersterk nepweb" 5701: 5524:Eisoldt, L.; Smith, A. & Scheibel, T. (2011). 4579: 3764: 3725: 3695:"control of drag-line spinning in certain spiders" 3399: 3048: 2917:"Overview of materials for AISI 4000 Series Steel" 2872: 2679:Journal of Polymer Science Part B: Polymer Physics 1028:2 coronate glands for the thread of adhesion lines 5555: 5553: 4769:"Materials: Surprising strength of silkworm silk" 4752:: CS1 maint: DOI inactive as of September 2024 ( 3992: 3592: 2989:"Materials: Surprising strength of silkworm silk" 1708:"Liquid Crystallinity of Natural Silk Secretions" 220:embedded in an amorphous matrix interlinked with 8102: 6913:Heimer, S. (1988). Wunderbare Welt der Spinnen. 3175: 2332:Heimer, S. (1988). Wunderbare Welt der Spinnen. 1691:"Spider silk as an archetypal protein elastomer" 6907: 5789: 5735:Proceedings of the National Academy of Sciences 3773: 3217: 3215: 3098: 3096: 1328:succeeded in making spider silk directly using 880: 874:Temporary scaffolding during web construction. 808:construction, defence, capturing and detaining 5550: 5401: 4502: 4500: 4444: 4263: 3947: 3639:Andersson, M; Johansson, J; Rising, A (2016). 3466: 3464: 3462: 3044: 3042: 3040: 2344: 2342: 1663:"Molecular Modeling of Spider Silk Elasticity" 1388:company Nexia produced spider silk protein in 298:. Spider silk is, however, tougher than both. 7560: 7262: 6198:Lucas, F. (1964). "Spiders and their silks". 5724: 5026: 5024: 4541: 3863:Eisoldt, L.; Smith, A.; Scheibel, T. (2011). 3814:Eisoldt, L.; Thamm, C.; Scheibel, T. (2012). 3692: 3495: 3397: 2959: 2193: 2191: 1970: 1968: 1768:First successful synthesis of Spider silk by 1649:"The structure and properties of spider silk" 468:, with some samples reaching 520 MJ/m. Thus, 7129:, a BBC program about silk-producing animals 6758: 5081: 5079: 4965: 4865: 4863: 3470: 3393: 3391: 3389: 3387: 3212: 3093: 2986: 2620: 2618: 2348: 2139: 2137: 2135: 2133: 1734:"Liquid crystalline spinning of spider silk" 1236: 333:(450−2000 MPa), and about half as strong as 7207:Victoria and Albert Museum (29 July 2019). 4869: 4497: 3688: 3686: 3645:International Journal of Molecular Sciences 3459: 3037: 2672: 2670: 2668: 2666: 2339: 2091: 2089: 2018: 7567: 7553: 7269: 7255: 6960:Journal of Cellular and Molecular Medicine 6761:"Spider silk cape goes on show at V&A" 5697: 5695: 5693: 5691: 5650:ACS Biomaterials Science & Engineering 5360:ACS Biomaterials Science & Engineering 5157: 5021: 4823: 4544:Quarterly Journal of Microscopical Science 3565: 2791:Journal of Materials Processing Technology 2188: 1965: 1931:Spider silk has been used as a thread for 1594:First X-ray on single spider silk fibres. 1416:Significant papers (50 or more citations) 1332:modified with certain genes of the spider 618:, and the "water" or "diving bell" spider 329:is comparable to that of high-grade alloy 161:), mainly consisting of highly repetitive 7160: 7150: 6979: 6795: 6626: 6599:Knight, D. P. & Vollrath, F. (1999). 6287: 6197: 6174: 6164: 5970: 5960: 5772: 5754: 5671: 5661: 5628: 5541: 5486: 5476: 5427: 5379: 5331: 5285: 5193: 5183: 5076: 4891: 4860: 4792: 4644: 4289: 4240: 4214: 4191: 4181: 4163: 4070: 3921: 3880: 3831: 3739: 3710: 3666: 3656: 3384: 3367: 3318: 3257: 3247: 3012: 2849: 2761: 2615: 2582: 2464: 2454: 2233: 2223: 2130: 2113: 2096:Hinman, M. B. & Lewis, R. V. (1992). 1995: 1926: 1025:4 aggregate glands for adhesive functions 1013:500 pyriform glands for attachment points 489:adhesive properties of the silk resemble 209:that would otherwise digest the protein. 149:Silks have a hierarchical structure. The 6026: 5942: 5704:"Spinning spider silk into startup gold" 3683: 3641:"Silk Spinning in Silkworms and Spiders" 3634: 3632: 3288: 3286: 3284: 2663: 2523: 2328: 2326: 2086: 1809: 1297: 1293: 1036: 955: 927: 884: 818: 701: 689: 285: 140: 41: 27: 7132: 7085: 6926: 6851: 5688: 4767:Shao, Z. Z. & Vollrath, F. (2002). 4377:Angewandte Chemie International Edition 3522: 1373:used research from the Universities of 1273:jump from their point of emission, the 1032: 657:, hang from a drop line while feeding. 345:silk has the highest tensile strength. 8103: 7177: 6777: 6683:Applied Microbiology and Biotechnology 5702:Service, Robert F. (18 October 2017). 5151: 2987:Shao, Zhengzhong; Vollrath, F (2002). 2962:"Material Tensile Strength Comparison" 1420: 1069:Average Maximum breaking stress (MPa) 960:Schematic of a generalised gland of a 855:Tubiliform (a.k.a. cylindriform) silk 451: 413: 7548: 7250: 7209:"How was it made? Golden spider silk" 6870: 6852:Leggett, Hadley (23 September 2009). 6027:Thompson, Bronwyn (22 January 2024). 5526:"Decoding the secrets of spider silk" 4128: 3865:"Decoding the secrets of spider silk" 3629: 3281: 2714: 2712: 2710: 2708: 2323: 1916:silk was used in research concerning 1755: 1698: 1639: 1540: 1482: 1437: 1216: 89:or other structures that function as 8085: 7107:"Material Properties of Spider Silk" 6007: 5402:Kinahan, M. E.; et al. (2011). 4264:Knight, D. P.; Vollrath, F. (1999). 3475:. London: New Holland. p. 160. 1796:"Artificial Spinning of Spider Silk" 1780:Arcidiacono, S., Kaplan, D.L. et al. 1324:In March 2010, researchers from the 1022:4 tubuliform glands for egg sac silk 1016:4 ampullate glands for the web frame 858:Protective egg sacs. Stiffest silk. 193:in aqueous solution, resulting in a 5853:. 29 September 2010. Archived from 4215:Kronqvist, N.; et al. (2014). 4164:Andersson, M.; et al. (2014). 3595:The Journal of Experimental Biology 1910:, which can aid in clotting blood. 1762:Prince, J. T., Kaplan, D. L. et al. 846:Capture-spiral (flagelliform) silk 442: 370:of dragline spider silk is roughly 320: 13: 7104: 6972:10.1111/j.1582-4934.2006.tb00436.x 6606:Proceedings of the Royal Society B 6267:Proceedings of the Royal Society B 6139:Xu, M. & Lewis, R. V. (1990). 5943:Scheibel, Thomas (November 2004). 4438: 3445:10.1146/annurev-ento-112408-085401 2705: 2387:Proceedings of the Royal Society B 1580:First Raman study of spider silk. 1264: 605:Nest lining and nest construction 304: 14: 8142: 7120: 4629:Journal of Visualized Experiments 1793:Seidel, A., Jelinski, L.W. et al. 1622:First X-ray on spider silk dope. 1602:Knight, D.P., Vollrath, F. et al. 1503:Vollrath, F. & Edmonds, D. T. 1113:Typical golden orb weaving spider 361: 8084: 8075: 8074: 7529: 7528: 7327: 7133:Meadows, Robin (5 August 2014). 7098: 7079: 7033: 7009: 6996: 6947: 6920: 6864: 6845: 6820: 6771: 6759:Maev Kennedy (24 January 2012). 6752: 6717: 6674: 6635: 6592: 6549: 6498: 6471: 6436: 6401: 6366: 6339: 6304: 6253: 6210: 6191: 6132: 6096: 6081: 6046: 6020: 5883:. 1 October 2010. Archived from 5158:Xia, X. X.; et al. (2010). 4987:Current Opinion in Plant Biology 3273: 2803:10.1016/j.jmatprotec.2015.08.024 2480: 1640:Structure-Property Relationship 1566:First NMR study of spider silk. 1252: 838:Major-ampullate (dragline) silk 246: 7178:Rejcek, Peter (11 April 2019). 6001: 5987: 5936: 5899: 5869: 5839: 5833:"Bolt Threads – B-silk protein" 5825: 5811: 5718: 5663:10.1021/acsbiomaterials.1c00612 5637: 5604: 5517: 5503: 5444: 5395: 5372:10.1021/acsbiomaterials.1c00612 5347: 5310: 5261: 5210: 5115: 4978: 4959: 4916: 4817: 4760: 4696: 4661: 4616: 4573: 4554: 4535: 4403: 4368: 4333: 4298: 4257: 4208: 4157: 4122: 4087: 4030: 3889: 3856: 3719: 3586: 3559: 3489: 3424: 3335: 3169: 3147: 2980: 2953: 2939:"DuPont Kevlar 49 Aramid Fiber" 2931: 2909: 2866: 2817: 2778: 2628:Journal of Experimental Biology 2562: 2488: 2422: 2377: 1731:Vollrath, F. & Knight, D.P. 1718:Knight, D.P. & Vollrath, F. 1280: 7086:Goodyer, Jason (5 July 2020). 6893:10.1103/PhysRevLett.108.154301 6828:"V&A · Golden spider silk" 2851:10.1088/1757-899X/987/1/012003 2287: 2250: 2039: 2012: 1946:Silk has been used to suspend 1941:N-slit interferometric signals 1900:used to cut up tubes built by 1844:The development of methods to 1547:Hinman, M.B. & Lewis, R. V 425: 1: 7065:10.1088/2040-8978/13/3/035710 6457:10.1016/S0141-8130(01)00166-0 6422:10.1016/S0141-8130(00)00124-0 6387:10.1016/S0141-8130(98)00084-1 6360:10.1016/S0032-3861(98)00475-3 6118:10.1016/S0022-2836(60)80045-9 5995:"Goldwin x Spiber Ski Jacket" 5922:10.1016/j.tibtech.2008.02.006 5617:Advanced Functional Materials 5543:10.1016/s1369-7021(11)70057-8 5320:Advanced Functional Materials 4726:(inactive 6 September 2024). 4521:10.1016/S0141-8130(98)00095-6 4063:10.1016/S0006-3495(96)79539-5 4016:10.1016/j.tibtech.2008.02.006 3882:10.1016/S1369-7021(11)70057-8 2960:Ganio Mego, Paolo (c. 2002). 2115:10.1016/S0021-9258(18)41777-2 1958: 1868:pumps, fashion clothing, and 1805: 1737:Most cited spider silk paper 1705:Kerkam, K., Kaplan, D. et al. 1688:Vollrath, F. & Porter, D. 1616:Riekel, C. & Vollrath, F. 1574:Shao, Z., Vollrath, F. et al. 1517:Vollrath, F. & Shao, Z.Z. 1444:Fischer, F. & Brander, J. 1410: 917: 685: 480:Silk fibre is a two-compound 259: 136: 131: 16:Protein fiber made by spiders 7152:10.1371/journal.pbio.1001922 6492:10.1016/0160-9327(86)90049-9 6106:Journal of Molecular Biology 4183:10.1371/journal.pbio.1001921 3914:10.1016/j.actbio.2013.08.020 3580:10.1002/scin.2007.5591711509 3506:10.1007/978-3-642-71552-5_15 3249:10.1371/journal.pone.0011234 2875:Journal of Materials Science 2456:10.1371/journal.pone.0000998 2204:Proc. Natl. Acad. Sci. U.S.A 1814:A cape made from Madagascar 1588:Riekel, C., Muller, M.et al. 1541:Structural Characterisation 1191:Tobacco & potato plants 1049: 1046:be synthesised into fibres. 881:Synthesis and fibre spinning 645:Drop lines and anchor lines 393: 381: 201:and thus protecting it from 197:of about 4, making the silk 187:Potassium hydrogen phosphate 7: 7366:List of families of spiders 7276: 7021:. Bonnier Corporation. 1955 6067:10.1515/bchm2.1960.320.1.92 5851:Kraig Biocraft Laboratories 3473:The Private Life of Spiders 3433:Annual Review of Entomology 3051:European Physical Journal E 2166:10.1126/science.271.5245.84 1948:inertial confinement fusion 1891: 1371:Kraig Biocraft Laboratories 1318: 1208: 718:jumps with safety line, on 475: 85:. Spiders use silk to make 10: 8147: 7574: 7004:Field Notes – Spin Control 6832:Victoria and Albert Museum 6008:Bain, Marc (3 July 2016). 5819:"Bolt Threads – Microsilk" 5731:results in a strong fiber" 4884:10.1021/acs.biomac.8b00980 3071:10.1140/epje/e2005-00021-2 2052:The Journal of Arachnology 1788: 1775: 1754: 1740: 1726: 1713: 1697: 1683: 1669: 1655: 1638: 1625: 1611: 1597: 1583: 1569: 1555: 1539: 1525: 1512: 1498: 1481: 1465: 1452: 1436: 1433:Contribution to the field 1419: 921: 672: 662: 643: 633: 603: 584: 571: 561: 539: 525: 514: 348: 157:sequence of its proteins ( 18: 8116:Animal glandular products 8070: 7959: 7926: 7878: 7855: 7846: 7824: 7711: 7591: 7582: 7524: 7503: 7472: 7379: 7336: 7325: 7284: 6784:Journal of Design History 5274:Macromolecular Bioscience 5007:10.1016/j.pbi.2005.01.010 4838:10.1007/s11033-009-9615-2 4826:Molecular Biology Reports 2601:10.1007/s00340-017-6766-z 2006:10.1017/S0952836903004540 1896:Peasants in the southern 1492:"Spiders and their silks" 1473:Xu, M. & Lewis, R. V. 1466: 1432: 1429: 1426: 1423: 1290:model of a blood vessel. 1244: 1237:Superhydrophobic surfaces 1190: 1174: 1146: 1125: 1078: 1071: 1068: 1065: 1062: 530:Orb webs produced by the 6778:Morgan, Eleanor (2016). 5949:Microbial Cell Factories 5881:University of Notre Dame 5510:Spintec Engineering GmbH 4967:US patent 2008109923 3534:26 November 2011 at the 3498:Ecophysiology of Spiders 1349:(1.03 ± 0.11 GPa), 577:"Ballooning" or "kiting" 283:a stress-strain curve). 7371:Lists of spider species 7135:"How Spiders Spin Silk" 6873:Physical Review Letters 6166:10.1073/pnas.87.18.7120 5909:Trends in Biotechnology 5756:10.1073/pnas.1003366107 5478:10.1073/pnas.0709246105 5185:10.1073/pnas.1003366107 5054:10.1126/science.1065780 4447:Die Naturwissenschaften 2842:2020MS&E..987a2003N 2297:Macromol. Rapid Commun. 1937:telescopic rifle sights 943:golden silk orb-weavers 906:. Silk production is a 504: 38:wraps her prey in silk. 6929:Journal of Arachnology 6619:10.1098/rspb.1999.0667 6445:Int. J. Biol. Macromol 6410:Int. J. Biol. Macromol 6375:Int. J. Biol. Macromol 6280:10.1098/rspb.2001.1590 5962:10.1186/1475-2859-3-14 5630:10.1002/adfm.202002982 5582:10.1002/adma.201704325 5333:10.1002/adfm.202002982 5287:10.1002/mabi.202200450 5239:10.1002/adma.201704325 4389:10.1002/anie.200803341 4282:10.1098/rspb.1999.0667 3693:Wilson, R. S. (1969). 3398:Foelix, R. F. (1996). 3198:10.1002/adma.200400344 2746:10.1126/sciadv.abo6043 2408:10.1098/rspb.1996.0023 2309:10.1002/marc.200900018 2225:10.1073/pnas.152162299 2064:10.1636/JoA-S-17-093.1 2021:Journal of Arachnology 1927:Science and technology 1819: 1630:Van Beek, J. D. et al. 1483:Mechanical Properties 1303: 1084:Darwin's bark spider ( 1042: 965: 962:Golden silk orb-weaver 934: 894: 824: 729: 699: 410:silk is the toughest. 291: 146: 64: 39: 21:Arachnidium (bryozoan) 6695:10.1007/s002530051133 4467:10.1007/s001140100220 3788:10.1038/nchembio.1789 3471:Hillyard, P. (2007). 3348:Nature Communications 1864:coatings, mechanical 1852:, athletic footwear, 1813: 1421:Area of contribution 1301: 1294:Synthetic spider silk 1040: 959: 952:Gland characteristics 931: 922:Further information: 888: 871:Minor-ampullate silk 822: 714: 693: 289: 144: 103:float through the air 45: 32:A female specimen of 31: 3728:Surf. Interface Anal 3658:10.3390/ijms17081290 3500:. pp. 211–225. 1898:Carpathian Mountains 1646:Gosline, G.M. et al. 1033:Artificial synthesis 648:Spiders such as the 611:Segestria florentina 541:Prey immobilisation 458:Darwin's bark spider 7485:Cultural depictions 7127:"The Silk Spinners" 7057:2011JOpt...13c5710D 7002:Berenbaum, May R., 6885:2012PhRvL.108o4301O 6738:1998MaMol..31.6733S 6660:10.1021/bi00034a022 6570:1991Natur.349..596K 6519:2006SMat....2..377V 6333:10.1021/ma00096a060 6325:1994MaMol..27.5235S 6231:1989Natur.340..305V 6157:1990PNAS...87.7120X 5747:2010PNAS..10714059X 5574:2018AdM....3004325G 5469:2008PNAS..105.6590R 5231:2018AdM....3004325G 5176:2010PNAS..10714059X 5137:2002MaMol..35.1262A 5101:2000MaMol..33..775S 5046:2002Sci...295..472L 4999:2005COPB....8..188S 4937:2011MaMol..44.1166E 4785:2002Natur.418..741S 4509:Int J Biol Macromol 4459:2001NW.....88..179K 4424:2002JChEd..79...10H 4233:2014NatCo...5.3254K 4055:1996BpJ....71.3442H 3962:2001Natur.410..541V 3712:10.1093/icb/9.1.103 3360:2012NatCo...3.1106S 3311:2015SMat...11.2394W 3240:2010PLoSO...511234A 3190:2005AdM....17...84Y 3117:2001Natur.410..541V 3063:2005EPJE...16..199P 3005:2002Natur.418..741S 2887:1980JMatS..15..491G 2738:2022SciA....8O6043A 2691:2006JPoSB..44..994P 2593:2017ApPhB.123..188Z 2548:2012SMat....8.6015P 2509:2005MaMol..38.8447S 2447:2007PLoSO...2..998S 2400:1996RSPSB.263..147V 2371:10.1021/ma00103a018 2363:1994MaMol..27.7378T 2216:2002PNAS...9910266V 2158:1996Sci...271...84S 1824:François Xavier Bon 1417: 1308:genetic engineering 1059: 914:of multiple types. 725:Misumessus oblongus 621:Argyroneta aquatica 452:Highest-performance 414:Elongation at break 337:filaments, such as 271:and extensibility ( 6797:10.1093/jdh/epv019 6092:. Symp. 3: 208–14. 5887:on 10 October 2010 5219:Advanced Materials 5170:(32): 14, 059–63. 4242:10.1038/ncomms4254 3601:(Pt 13): 2452–61. 3402:Biology of Spiders 3369:10.1038/ncomms2099 3320:10.1039/c4sm02130d 3178:Advanced Materials 2968:on 26 October 2009 2895:10.1007/BF00551703 2699:10.1002/polb.20751 2556:10.1039/C2SM25446H 1984:Journal of Zoology 1886:golden orb spiders 1820: 1674:Simmons, A. et al. 1560:Simmons, A. et al. 1415: 1304: 1217:Syringe and needle 1086:Caerostris darwini 1058: 1043: 1006:Araneus diadematus 966: 935: 895: 825: 755:Ampullate (minor) 747:Ampullate (major) 730: 700: 674:Pheromonal trails 462:Caerostris darwini 420:Caerostris darwini 325:A dragline silk's 315:Ariadna lateralisl 292: 234:neutron scattering 147: 65: 40: 35:Argiope bruennichi 8111:Materials science 8098: 8097: 8066: 8065: 7842: 7841: 7542: 7541: 7473:Human interaction 7092:BBC Science Focus 7045:Journal of Optics 6746:10.1021/ma9808880 6274:(1483): 2339–46. 5879:(Press release). 5849:(Press release). 5420:10.1021/bm1014624 5408:Biomacromolecules 5145:10.1021/ma011471o 5109:10.1021/ma990893j 4945:10.1021/ma102291m 4872:Biomacromolecules 4682:10.1021/bm900312c 4670:Biomacromolecules 4594:10.1021/bm0156126 4582:Biomacromolecules 4354:10.1021/bm800390j 4342:Biomacromolecules 4319:10.1021/bm701069y 4307:Biomacromolecules 4143:10.1021/cr010194g 4108:10.1021/bm800390j 4096:Biomacromolecules 4004:Trends Biotechnol 3833:10.1002/bip.22006 3607:10.1242/jeb.02275 3515:978-3-642-71554-9 3482:978-1-84537-690-1 3417:978-0-19-509594-4 2641:10.1242/jeb.01344 2571:Applied Physics B 2517:10.1021/ma0507995 2273:10.1021/bm700877g 2260:Biomacromolecules 1832:Ramón M. Termeyer 1816:golden orb spider 1803: 1802: 1427:Main researchers 1384:Defunct Canadian 1206: 1205: 878: 877: 802: 801: 712: 683: 682: 439:for spider silk. 408:Araneus ishisawai 211:Potassium nitrate 151:primary structure 8138: 8088: 8087: 8078: 8077: 7853: 7852: 7589: 7588: 7569: 7562: 7555: 7546: 7545: 7532: 7531: 7331: 7271: 7264: 7257: 7248: 7247: 7243: 7241: 7239: 7223: 7221: 7219: 7194: 7192: 7190: 7174: 7164: 7154: 7114: 7113: 7111: 7105:Bonino, Mark J. 7102: 7096: 7095: 7083: 7077: 7076: 7037: 7031: 7030: 7028: 7026: 7013: 7007: 7000: 6994: 6993: 6983: 6951: 6945: 6944: 6924: 6918: 6911: 6905: 6904: 6868: 6862: 6861: 6849: 6843: 6842: 6840: 6838: 6824: 6818: 6817: 6799: 6775: 6769: 6768: 6756: 6750: 6749: 6721: 6715: 6714: 6678: 6672: 6671: 6654:(34): 10879–85. 6639: 6633: 6632: 6630: 6613:(1418): 519–23. 6596: 6590: 6589: 6578:10.1038/349596a0 6564:(6310): 596–98. 6553: 6547: 6546: 6527:10.1039/b600098n 6502: 6496: 6495: 6475: 6469: 6468: 6440: 6434: 6433: 6405: 6399: 6398: 6370: 6364: 6363: 6354:(10): 2493–500. 6343: 6337: 6336: 6308: 6302: 6301: 6291: 6257: 6251: 6250: 6239:10.1038/340305a0 6225:(6231): 305–07. 6214: 6208: 6207: 6195: 6189: 6188: 6178: 6168: 6136: 6130: 6129: 6100: 6094: 6093: 6090:Insect Chemistry 6085: 6079: 6078: 6050: 6044: 6043: 6041: 6039: 6024: 6018: 6017: 6005: 5999: 5998: 5991: 5985: 5984: 5974: 5964: 5940: 5934: 5933: 5903: 5897: 5896: 5894: 5892: 5873: 5867: 5866: 5864: 5862: 5843: 5837: 5836: 5829: 5823: 5822: 5815: 5809: 5808: 5806: 5804: 5793: 5787: 5786: 5776: 5758: 5741:(32): 14059–63. 5729:Escherichia coli 5722: 5716: 5715: 5713: 5711: 5699: 5686: 5685: 5675: 5665: 5656:(7): 3332–3339. 5641: 5635: 5634: 5632: 5608: 5602: 5601: 5557: 5548: 5547: 5545: 5521: 5515: 5514: 5507: 5501: 5500: 5490: 5480: 5448: 5442: 5441: 5431: 5399: 5393: 5392: 5383: 5366:(7): 3332–3339, 5351: 5345: 5344: 5335: 5314: 5308: 5307: 5289: 5265: 5259: 5258: 5214: 5208: 5207: 5197: 5187: 5155: 5149: 5148: 5119: 5113: 5112: 5083: 5074: 5073: 5040:(5554): 472–76. 5028: 5019: 5018: 4982: 4976: 4975: 4974: 4970: 4963: 4957: 4956: 4920: 4914: 4913: 4895: 4893:2060/20180007385 4867: 4858: 4857: 4821: 4815: 4814: 4796: 4764: 4758: 4757: 4751: 4743: 4724:10.1554/06-267.1 4709: 4700: 4694: 4693: 4665: 4659: 4658: 4648: 4620: 4614: 4613: 4577: 4571: 4570: 4558: 4552: 4551: 4539: 4533: 4532: 4504: 4495: 4494: 4442: 4436: 4435: 4432:10.1021/ed079p10 4407: 4401: 4400: 4372: 4366: 4365: 4337: 4331: 4330: 4302: 4296: 4295: 4293: 4276:(1418): 519–23. 4261: 4255: 4254: 4244: 4212: 4206: 4205: 4195: 4185: 4161: 4155: 4154: 4126: 4120: 4119: 4091: 4085: 4084: 4074: 4034: 4028: 4027: 3999: 3990: 3989: 3970:10.1038/35069000 3956:(6828): 541–48. 3945: 3936: 3935: 3925: 3893: 3887: 3886: 3884: 3860: 3854: 3853: 3835: 3811: 3800: 3799: 3771: 3762: 3761: 3750:10.1002/sia.6545 3743: 3723: 3717: 3716: 3714: 3690: 3681: 3680: 3670: 3660: 3636: 3627: 3626: 3590: 3584: 3583: 3563: 3557: 3554: 3539: 3526: 3520: 3519: 3493: 3487: 3486: 3468: 3457: 3456: 3428: 3422: 3421: 3405: 3395: 3382: 3381: 3371: 3339: 3333: 3332: 3322: 3305:(12): 2394–403. 3290: 3279: 3278: 3277: 3271: 3261: 3251: 3219: 3210: 3209: 3173: 3167: 3166: 3164: 3162: 3157:. chm.bris.ac.uk 3151: 3145: 3144: 3125:10.1038/35069000 3111:(6828): 541–48. 3100: 3091: 3090: 3046: 3035: 3034: 3016: 2984: 2978: 2977: 2975: 2973: 2964:. Archived from 2957: 2951: 2950: 2948: 2946: 2935: 2929: 2928: 2926: 2924: 2913: 2907: 2906: 2870: 2864: 2863: 2853: 2821: 2815: 2814: 2782: 2776: 2775: 2765: 2732:(41): eabo6043. 2726:Science Advances 2716: 2703: 2702: 2674: 2661: 2660: 2622: 2613: 2612: 2586: 2566: 2560: 2559: 2527: 2521: 2520: 2492: 2486: 2485: 2484: 2478: 2468: 2458: 2426: 2420: 2419: 2394:(1367): 147–51. 2381: 2375: 2374: 2346: 2337: 2330: 2321: 2320: 2303:(9–10): 851–57. 2291: 2285: 2284: 2254: 2248: 2247: 2237: 2227: 2210:(16): 10266–71. 2195: 2186: 2185: 2141: 2128: 2127: 2117: 2108:(27): 19320–24. 2093: 2084: 2083: 2043: 2037: 2036: 2016: 2010: 2009: 1999: 1981: 1972: 1850:ballistic armour 1840: 1699:Native Spinning 1457:Lucas, F. et al. 1418: 1414: 1347:tensile strength 1335:Nephila clavipes 1149:Escherichia coli 1109:Nephila clavipes 1060: 1057: 893:spinning its web 827: 826: 790:Sticky globules 736: 735: 713: 548:. In species of 513: 512: 493:, consisting of 443:Supercontraction 433:glass transition 377: 375: 327:tensile strength 321:Tensile strength 269:tensile strength 250: 171:block co-polymer 53:Józef Chełmoński 8146: 8145: 8141: 8140: 8139: 8137: 8136: 8135: 8101: 8100: 8099: 8094: 8062: 7955: 7922: 7874: 7865:Artificial silk 7838: 7820: 7707: 7578: 7573: 7543: 7538: 7520: 7516:Web decorations 7499: 7495:Spider fighting 7468: 7464:Urticating hair 7414:Cheliceral fang 7375: 7332: 7323: 7280: 7275: 7237: 7235: 7226: 7217: 7215: 7203:Wayback Machine 7188: 7186: 7184:Singularity Hub 7145:(8): e1001922. 7123: 7118: 7117: 7109: 7103: 7099: 7084: 7080: 7038: 7034: 7024: 7022: 7015: 7014: 7010: 7001: 6997: 6952: 6948: 6925: 6921: 6912: 6908: 6869: 6865: 6850: 6846: 6836: 6834: 6826: 6825: 6821: 6776: 6772: 6757: 6753: 6732:(19): 6733–36. 6722: 6718: 6679: 6675: 6640: 6636: 6597: 6593: 6554: 6550: 6503: 6499: 6476: 6472: 6441: 6437: 6406: 6402: 6381:(2–3): 179–86. 6371: 6367: 6344: 6340: 6319:(18): 5235–37. 6309: 6305: 6258: 6254: 6215: 6211: 6196: 6192: 6151:(18): 7120–24. 6137: 6133: 6101: 6097: 6086: 6082: 6051: 6047: 6037: 6035: 6025: 6021: 6006: 6002: 5993: 5992: 5988: 5941: 5937: 5904: 5900: 5890: 5888: 5875: 5874: 5870: 5860: 5858: 5845: 5844: 5840: 5831: 5830: 5826: 5817: 5816: 5812: 5802: 5800: 5795: 5794: 5790: 5723: 5719: 5709: 5707: 5700: 5689: 5642: 5638: 5623:(40): 2002982. 5609: 5605: 5558: 5551: 5522: 5518: 5512: 5508: 5504: 5463:(18): 6590–95. 5449: 5445: 5400: 5396: 5352: 5348: 5315: 5311: 5280:(4): e2200450. 5266: 5262: 5215: 5211: 5156: 5152: 5120: 5116: 5084: 5077: 5029: 5022: 4983: 4979: 4972: 4964: 4960: 4921: 4917: 4868: 4861: 4822: 4818: 4794:10.1038/418741a 4765: 4761: 4745: 4744: 4718:(12): 2539–51. 4707: 4701: 4697: 4666: 4662: 4621: 4617: 4578: 4574: 4559: 4555: 4540: 4536: 4515:(2–3): 243–49. 4505: 4498: 4443: 4439: 4408: 4404: 4383:(20): 3584–96. 4373: 4369: 4348:(9): 2399–407. 4338: 4334: 4303: 4299: 4270:Proc. R. Soc. B 4262: 4258: 4213: 4209: 4176:(8): e1001921. 4162: 4158: 4127: 4123: 4102:(9): 2399–407. 4092: 4088: 4035: 4031: 4000: 3993: 3946: 3939: 3894: 3890: 3861: 3857: 3812: 3803: 3776:Nat. Chem. Biol 3772: 3765: 3724: 3720: 3691: 3684: 3637: 3630: 3591: 3587: 3564: 3560: 3555: 3542: 3536:Wayback Machine 3527: 3523: 3516: 3494: 3490: 3483: 3469: 3460: 3429: 3425: 3418: 3396: 3385: 3340: 3336: 3291: 3282: 3272: 3220: 3213: 3174: 3170: 3160: 3158: 3153: 3152: 3148: 3101: 3094: 3047: 3038: 3014:10.1038/418741a 2985: 2981: 2971: 2969: 2958: 2954: 2944: 2942: 2937: 2936: 2932: 2922: 2920: 2915: 2914: 2910: 2871: 2867: 2822: 2818: 2783: 2779: 2717: 2706: 2675: 2664: 2623: 2616: 2567: 2563: 2542:(22): 6015–26. 2528: 2524: 2493: 2489: 2479: 2427: 2423: 2382: 2378: 2357:(25): 7378–81. 2347: 2340: 2331: 2324: 2292: 2288: 2255: 2251: 2196: 2189: 2152:(5245): 84–87. 2142: 2131: 2094: 2087: 2044: 2040: 2017: 2013: 1997:10.1.1.536.9091 1979: 1973: 1966: 1961: 1929: 1894: 1834: 1808: 1438:Chemical Basis 1413: 1363:using bacteria. 1321: 1296: 1283: 1270:Electrospinning 1267: 1265:Electrospinning 1255: 1247: 1239: 1219: 1211: 1052: 1035: 926: 920: 904:spinning wheels 883: 863:Aciniform silk 720:yellow ironweed 702: 688: 591:kleptoparasitic 507: 478: 454: 445: 428: 416: 396: 384: 373: 371: 364: 351: 323: 310:Young's modulus 307: 305:Young's modulus 262: 255: 251: 241: 139: 134: 57:National Museum 24: 17: 12: 11: 5: 8144: 8134: 8133: 8131:Spider anatomy 8128: 8123: 8118: 8113: 8096: 8095: 8093: 8092: 8082: 8071: 8068: 8067: 8064: 8063: 8061: 8060: 8055: 8050: 8045: 8040: 8035: 8034: 8033: 8023: 8018: 8013: 8008: 8003: 7998: 7997: 7996: 7991: 7986: 7981: 7971: 7965: 7963: 7957: 7956: 7954: 7953: 7948: 7943: 7938: 7932: 7930: 7924: 7923: 7921: 7920: 7915: 7910: 7905: 7900: 7895: 7890: 7884: 7882: 7880:Semi-synthetic 7876: 7875: 7873: 7872: 7867: 7861: 7859: 7850: 7844: 7843: 7840: 7839: 7837: 7836: 7830: 7828: 7822: 7821: 7819: 7818: 7813: 7808: 7803: 7798: 7793: 7788: 7783: 7778: 7773: 7768: 7763: 7758: 7753: 7748: 7743: 7738: 7733: 7728: 7723: 7717: 7715: 7709: 7708: 7706: 7705: 7700: 7695: 7690: 7685: 7680: 7675: 7670: 7665: 7660: 7655: 7650: 7645: 7644: 7643: 7633: 7628: 7623: 7618: 7613: 7608: 7603: 7597: 7595: 7586: 7580: 7579: 7572: 7571: 7564: 7557: 7549: 7540: 7539: 7537: 7536: 7525: 7522: 7521: 7519: 7518: 7513: 7507: 7505: 7501: 7500: 7498: 7497: 7492: 7487: 7482: 7476: 7474: 7470: 7469: 7467: 7466: 7461: 7456: 7451: 7446: 7441: 7436: 7431: 7426: 7421: 7416: 7411: 7406: 7401: 7396: 7391: 7385: 7383: 7377: 7376: 7374: 7373: 7368: 7363: 7358: 7353: 7348: 7342: 7340: 7334: 7333: 7326: 7324: 7322: 7321: 7316: 7314:Classification 7311: 7306: 7301: 7296: 7290: 7288: 7282: 7281: 7274: 7273: 7266: 7259: 7251: 7245: 7244: 7234:. 21 July 2021 7224: 7195: 7175: 7130: 7122: 7121:External links 7119: 7116: 7115: 7097: 7078: 7032: 7008: 6995: 6946: 6919: 6906: 6879:(15): 154301. 6863: 6844: 6819: 6770: 6751: 6726:Macromolecules 6716: 6673: 6634: 6591: 6548: 6497: 6470: 6435: 6400: 6365: 6338: 6313:Macromolecules 6303: 6252: 6209: 6190: 6131: 6095: 6080: 6045: 6019: 6000: 5986: 5935: 5898: 5868: 5857:on 25 May 2011 5838: 5824: 5810: 5788: 5717: 5687: 5636: 5603: 5568:(3): 1704325. 5549: 5516: 5502: 5443: 5414:(5): 1504–11. 5394: 5346: 5309: 5260: 5209: 5150: 5131:(4): 1262–66. 5125:Macromolecules 5114: 5089:Macromolecules 5075: 5020: 4977: 4958: 4931:(5): 1166–76. 4925:Macromolecules 4915: 4878:(9): 3853–60. 4859: 4832:(4): 1815–21. 4816: 4759: 4695: 4676:(7): 1904–10. 4660: 4615: 4572: 4553: 4534: 4496: 4437: 4402: 4367: 4332: 4297: 4256: 4207: 4156: 4137:(9): 3762–74. 4121: 4086: 4049:(6): 3442–47. 4029: 3991: 3937: 3908:(4): 1612–26. 3888: 3855: 3801: 3763: 3718: 3682: 3628: 3585: 3574:(15): 231–34. 3558: 3540: 3521: 3514: 3488: 3481: 3458: 3423: 3416: 3383: 3334: 3280: 3211: 3168: 3146: 3092: 3057:(2): 199–206. 3036: 2979: 2952: 2930: 2908: 2865: 2816: 2777: 2704: 2662: 2614: 2561: 2522: 2497:Macromolecules 2487: 2421: 2376: 2351:Macromolecules 2338: 2322: 2286: 2249: 2187: 2129: 2085: 2058:(2): 173–206. 2038: 2011: 1963: 1962: 1960: 1957: 1928: 1925: 1923:regeneration. 1893: 1890: 1858:breast implant 1807: 1804: 1801: 1800: 1797: 1794: 1791: 1787: 1786: 1784: 1781: 1778: 1774: 1773: 1766: 1763: 1760: 1757: 1753: 1752: 1749: 1746: 1743: 1739: 1738: 1735: 1732: 1729: 1725: 1724: 1722: 1719: 1716: 1712: 1711: 1709: 1706: 1703: 1700: 1696: 1695: 1692: 1689: 1686: 1682: 1681: 1678: 1675: 1672: 1668: 1667: 1664: 1661: 1658: 1654: 1653: 1650: 1647: 1644: 1641: 1637: 1636: 1634: 1631: 1628: 1624: 1623: 1620: 1617: 1614: 1610: 1609: 1606: 1603: 1600: 1596: 1595: 1592: 1589: 1586: 1582: 1581: 1578: 1575: 1572: 1568: 1567: 1564: 1561: 1558: 1554: 1553: 1551: 1548: 1545: 1542: 1538: 1537: 1534: 1531: 1528: 1524: 1523: 1521: 1518: 1515: 1511: 1510: 1507: 1504: 1501: 1497: 1496: 1493: 1490: 1487: 1484: 1480: 1479: 1477: 1474: 1471: 1468: 1467:Gene Sequence 1464: 1463: 1461: 1458: 1455: 1451: 1450: 1448: 1445: 1442: 1439: 1435: 1434: 1431: 1428: 1425: 1422: 1412: 1409: 1408: 1407: 1403: 1400: 1382: 1368: 1364: 1354: 1339: 1320: 1317: 1295: 1292: 1282: 1279: 1266: 1263: 1254: 1251: 1246: 1243: 1238: 1235: 1218: 1215: 1210: 1207: 1204: 1203: 1201: 1198: 1195: 1192: 1188: 1187: 1185: 1182: 1179: 1176: 1172: 1171: 1169: 1166: 1163: 1152: 1144: 1143: 1141: 1138: 1135: 1132: 1123: 1122: 1120: 1117: 1114: 1111: 1105: 1104: 1102: 1099: 1096: 1089: 1081: 1080: 1077: 1070: 1067: 1064: 1051: 1048: 1034: 1031: 1030: 1029: 1026: 1023: 1020: 1017: 1014: 998:liquid crystal 994: 993: 985: 977: 974: 971: 954: 953: 924:Spider anatomy 919: 916: 882: 879: 876: 875: 872: 868: 867: 864: 860: 859: 856: 852: 851: 847: 843: 842: 839: 835: 834: 831: 800: 799: 796: 792: 791: 788: 784: 783: 780: 776: 775: 772: 768: 767: 764: 760: 759: 756: 752: 751: 748: 744: 743: 740: 687: 684: 681: 680: 678: 675: 671: 670: 668: 665: 661: 660: 658: 646: 642: 641: 639: 636: 632: 631: 629: 606: 602: 601: 599: 587: 583: 582: 580: 574: 570: 569: 567: 564: 560: 559: 557: 542: 538: 537: 535: 528: 524: 523: 520: 517: 506: 503: 477: 474: 453: 450: 444: 441: 427: 424: 415: 412: 395: 392: 383: 380: 368:energy density 363: 362:Energy density 360: 350: 347: 343:Clubiona vigil 322: 319: 306: 303: 261: 258: 257: 256: 252: 245: 222:hydrogen bonds 138: 135: 133: 130: 126:sex pheromones 15: 9: 6: 4: 3: 2: 8143: 8132: 8129: 8127: 8124: 8122: 8119: 8117: 8114: 8112: 8109: 8108: 8106: 8091: 8083: 8081: 8073: 8072: 8069: 8059: 8056: 8054: 8051: 8049: 8046: 8044: 8041: 8039: 8036: 8032: 8029: 8028: 8027: 8024: 8022: 8019: 8017: 8014: 8012: 8009: 8007: 8004: 8002: 7999: 7995: 7992: 7990: 7987: 7985: 7982: 7980: 7977: 7976: 7975: 7972: 7970: 7967: 7966: 7964: 7962: 7958: 7952: 7949: 7947: 7944: 7942: 7939: 7937: 7934: 7933: 7931: 7929: 7925: 7919: 7916: 7914: 7911: 7909: 7906: 7904: 7901: 7899: 7896: 7894: 7891: 7889: 7886: 7885: 7883: 7881: 7877: 7871: 7868: 7866: 7863: 7862: 7860: 7858: 7854: 7851: 7849: 7845: 7835: 7832: 7831: 7829: 7827: 7823: 7817: 7814: 7812: 7809: 7807: 7804: 7802: 7799: 7797: 7794: 7792: 7789: 7787: 7784: 7782: 7779: 7777: 7774: 7772: 7769: 7767: 7764: 7762: 7759: 7757: 7754: 7752: 7749: 7747: 7744: 7742: 7739: 7737: 7734: 7732: 7729: 7727: 7724: 7722: 7719: 7718: 7716: 7714: 7710: 7704: 7701: 7699: 7696: 7694: 7691: 7689: 7686: 7684: 7681: 7679: 7676: 7674: 7671: 7669: 7666: 7664: 7661: 7659: 7656: 7654: 7651: 7649: 7646: 7642: 7639: 7638: 7637: 7634: 7632: 7629: 7627: 7624: 7622: 7619: 7617: 7614: 7612: 7609: 7607: 7604: 7602: 7599: 7598: 7596: 7594: 7590: 7587: 7585: 7581: 7577: 7570: 7565: 7563: 7558: 7556: 7551: 7550: 7547: 7535: 7527: 7526: 7523: 7517: 7514: 7512: 7509: 7508: 7506: 7502: 7496: 7493: 7491: 7488: 7486: 7483: 7481: 7480:Arachnophobia 7478: 7477: 7475: 7471: 7465: 7462: 7460: 7457: 7455: 7452: 7450: 7447: 7445: 7442: 7440: 7437: 7435: 7432: 7430: 7427: 7425: 7422: 7420: 7417: 7415: 7412: 7410: 7407: 7405: 7404:Cephalothorax 7402: 7400: 7397: 7395: 7392: 7390: 7389:Arthropod leg 7387: 7386: 7384: 7382: 7378: 7372: 7369: 7367: 7364: 7362: 7361:Opisthothelae 7359: 7357: 7356:Mygalomorphae 7354: 7352: 7349: 7347: 7346:Araneomorphae 7344: 7343: 7341: 7339: 7335: 7330: 7320: 7317: 7315: 7312: 7310: 7307: 7305: 7302: 7300: 7297: 7295: 7292: 7291: 7289: 7287: 7283: 7279: 7272: 7267: 7265: 7260: 7258: 7253: 7252: 7249: 7233: 7229: 7225: 7214: 7210: 7204: 7200: 7196: 7185: 7181: 7176: 7172: 7168: 7163: 7158: 7153: 7148: 7144: 7140: 7136: 7131: 7128: 7125: 7124: 7108: 7101: 7093: 7089: 7082: 7074: 7070: 7066: 7062: 7058: 7054: 7050: 7046: 7042: 7036: 7020: 7019: 7012: 7005: 6999: 6991: 6987: 6982: 6977: 6973: 6969: 6966:(3): 770–77. 6965: 6961: 6957: 6950: 6942: 6938: 6934: 6930: 6923: 6916: 6910: 6902: 6898: 6894: 6890: 6886: 6882: 6878: 6874: 6867: 6859: 6855: 6848: 6833: 6829: 6823: 6815: 6811: 6807: 6803: 6798: 6793: 6789: 6785: 6781: 6774: 6766: 6762: 6755: 6747: 6743: 6739: 6735: 6731: 6727: 6720: 6712: 6708: 6704: 6700: 6696: 6692: 6688: 6684: 6677: 6669: 6665: 6661: 6657: 6653: 6649: 6645: 6644:Kaplan, D. L. 6638: 6629: 6624: 6620: 6616: 6612: 6608: 6607: 6602: 6595: 6587: 6583: 6579: 6575: 6571: 6567: 6563: 6559: 6552: 6544: 6540: 6536: 6532: 6528: 6524: 6520: 6516: 6513:(5): 377–85. 6512: 6508: 6501: 6493: 6489: 6485: 6481: 6474: 6466: 6462: 6458: 6454: 6451:(3): 203–10. 6450: 6446: 6439: 6431: 6427: 6423: 6419: 6416:(3): 205–10. 6415: 6411: 6404: 6396: 6392: 6388: 6384: 6380: 6376: 6369: 6361: 6357: 6353: 6349: 6342: 6334: 6330: 6326: 6322: 6318: 6314: 6307: 6299: 6295: 6290: 6285: 6281: 6277: 6273: 6269: 6268: 6263: 6256: 6248: 6244: 6240: 6236: 6232: 6228: 6224: 6220: 6213: 6205: 6201: 6194: 6186: 6182: 6177: 6172: 6167: 6162: 6158: 6154: 6150: 6146: 6142: 6135: 6127: 6123: 6119: 6115: 6112:(6): 339–49. 6111: 6107: 6099: 6091: 6084: 6076: 6072: 6068: 6064: 6060: 6056: 6049: 6034: 6030: 6023: 6015: 6011: 6004: 5996: 5990: 5982: 5978: 5973: 5968: 5963: 5958: 5954: 5950: 5946: 5939: 5931: 5927: 5923: 5919: 5916:(5): 244–51. 5915: 5911: 5910: 5902: 5886: 5882: 5878: 5872: 5856: 5852: 5848: 5842: 5834: 5828: 5820: 5814: 5798: 5792: 5784: 5780: 5775: 5770: 5766: 5762: 5757: 5752: 5748: 5744: 5740: 5736: 5732: 5730: 5721: 5705: 5698: 5696: 5694: 5692: 5683: 5679: 5674: 5669: 5664: 5659: 5655: 5651: 5647: 5640: 5631: 5626: 5622: 5618: 5614: 5607: 5599: 5595: 5591: 5587: 5583: 5579: 5575: 5571: 5567: 5563: 5556: 5554: 5544: 5539: 5535: 5531: 5527: 5520: 5511: 5506: 5498: 5494: 5489: 5484: 5479: 5474: 5470: 5466: 5462: 5458: 5454: 5447: 5439: 5435: 5430: 5425: 5421: 5417: 5413: 5409: 5405: 5398: 5391: 5387: 5382: 5377: 5373: 5369: 5365: 5361: 5357: 5350: 5343: 5339: 5334: 5329: 5325: 5321: 5313: 5305: 5301: 5297: 5293: 5288: 5283: 5279: 5275: 5271: 5264: 5256: 5252: 5248: 5244: 5240: 5236: 5232: 5228: 5224: 5220: 5213: 5205: 5201: 5196: 5191: 5186: 5181: 5177: 5173: 5169: 5165: 5161: 5154: 5146: 5142: 5138: 5134: 5130: 5126: 5118: 5110: 5106: 5102: 5098: 5095:(3): 775–80. 5094: 5090: 5082: 5080: 5071: 5067: 5063: 5059: 5055: 5051: 5047: 5043: 5039: 5035: 5027: 5025: 5016: 5012: 5008: 5004: 5000: 4996: 4993:(2): 188–96. 4992: 4988: 4981: 4968: 4962: 4954: 4950: 4946: 4942: 4938: 4934: 4930: 4926: 4919: 4911: 4907: 4903: 4899: 4894: 4889: 4885: 4881: 4877: 4873: 4866: 4864: 4855: 4851: 4847: 4843: 4839: 4835: 4831: 4827: 4820: 4812: 4808: 4804: 4800: 4795: 4790: 4786: 4782: 4779:(6899): 741. 4778: 4774: 4770: 4763: 4755: 4749: 4741: 4737: 4733: 4729: 4725: 4721: 4717: 4713: 4706: 4699: 4691: 4687: 4683: 4679: 4675: 4671: 4664: 4656: 4652: 4647: 4642: 4638: 4634: 4630: 4626: 4619: 4611: 4607: 4603: 4599: 4595: 4591: 4588:(4): 644–48. 4587: 4583: 4576: 4568: 4564: 4563:Polym. Commun 4557: 4549: 4545: 4538: 4530: 4526: 4522: 4518: 4514: 4510: 4503: 4501: 4492: 4488: 4484: 4480: 4476: 4472: 4468: 4464: 4460: 4456: 4453:(4): 179–82. 4452: 4448: 4441: 4433: 4429: 4425: 4421: 4417: 4413: 4412:J. Chem. Educ 4406: 4398: 4394: 4390: 4386: 4382: 4378: 4371: 4363: 4359: 4355: 4351: 4347: 4343: 4336: 4328: 4324: 4320: 4316: 4313:(1): 216–21. 4312: 4308: 4301: 4292: 4287: 4283: 4279: 4275: 4271: 4267: 4260: 4252: 4248: 4243: 4238: 4234: 4230: 4226: 4222: 4218: 4211: 4203: 4199: 4194: 4189: 4184: 4179: 4175: 4171: 4167: 4160: 4152: 4148: 4144: 4140: 4136: 4132: 4125: 4117: 4113: 4109: 4105: 4101: 4097: 4090: 4082: 4078: 4073: 4068: 4064: 4060: 4056: 4052: 4048: 4044: 4040: 4033: 4025: 4021: 4017: 4013: 4010:(5): 244–51. 4009: 4005: 3998: 3996: 3987: 3983: 3979: 3975: 3971: 3967: 3963: 3959: 3955: 3951: 3944: 3942: 3933: 3929: 3924: 3919: 3915: 3911: 3907: 3903: 3902:Acta Biomater 3899: 3892: 3883: 3878: 3874: 3870: 3866: 3859: 3851: 3847: 3843: 3839: 3834: 3829: 3826:(6): 355–61. 3825: 3821: 3817: 3810: 3808: 3806: 3797: 3793: 3789: 3785: 3782:(5): 309–15. 3781: 3777: 3770: 3768: 3759: 3755: 3751: 3747: 3742: 3737: 3733: 3729: 3722: 3713: 3708: 3704: 3700: 3696: 3689: 3687: 3678: 3674: 3669: 3664: 3659: 3654: 3650: 3646: 3642: 3635: 3633: 3624: 3620: 3616: 3612: 3608: 3604: 3600: 3596: 3589: 3581: 3577: 3573: 3569: 3562: 3553: 3551: 3549: 3547: 3545: 3537: 3533: 3530: 3525: 3517: 3511: 3507: 3503: 3499: 3492: 3484: 3478: 3474: 3467: 3465: 3463: 3454: 3450: 3446: 3442: 3438: 3434: 3427: 3419: 3413: 3409: 3404: 3403: 3394: 3392: 3390: 3388: 3379: 3375: 3370: 3365: 3361: 3357: 3353: 3349: 3345: 3338: 3330: 3326: 3321: 3316: 3312: 3308: 3304: 3300: 3296: 3289: 3287: 3285: 3276: 3269: 3265: 3260: 3255: 3250: 3245: 3241: 3237: 3233: 3229: 3225: 3218: 3216: 3207: 3203: 3199: 3195: 3191: 3187: 3183: 3179: 3172: 3156: 3155:"Spider Silk" 3150: 3142: 3138: 3134: 3130: 3126: 3122: 3118: 3114: 3110: 3106: 3099: 3097: 3088: 3084: 3080: 3076: 3072: 3068: 3064: 3060: 3056: 3052: 3045: 3043: 3041: 3032: 3028: 3024: 3020: 3015: 3010: 3006: 3002: 2999:(6899): 741. 2998: 2994: 2990: 2983: 2967: 2963: 2956: 2940: 2934: 2918: 2912: 2904: 2900: 2896: 2892: 2888: 2884: 2881:(2): 491–96. 2880: 2876: 2869: 2861: 2857: 2852: 2847: 2843: 2839: 2836:(1): 012003. 2835: 2831: 2827: 2820: 2812: 2808: 2804: 2800: 2796: 2792: 2788: 2781: 2773: 2769: 2764: 2759: 2755: 2751: 2747: 2743: 2739: 2735: 2731: 2727: 2723: 2715: 2713: 2711: 2709: 2700: 2696: 2692: 2688: 2685:(6): 994–99. 2684: 2680: 2673: 2671: 2669: 2667: 2658: 2654: 2650: 2646: 2642: 2638: 2634: 2630: 2629: 2621: 2619: 2610: 2606: 2602: 2598: 2594: 2590: 2585: 2580: 2576: 2572: 2565: 2557: 2553: 2549: 2545: 2541: 2537: 2533: 2526: 2518: 2514: 2510: 2506: 2502: 2498: 2491: 2483: 2476: 2472: 2467: 2462: 2457: 2452: 2448: 2444: 2440: 2436: 2432: 2425: 2417: 2413: 2409: 2405: 2401: 2397: 2393: 2389: 2388: 2380: 2372: 2368: 2364: 2360: 2356: 2352: 2345: 2343: 2335: 2329: 2327: 2318: 2314: 2310: 2306: 2302: 2299: 2298: 2290: 2282: 2278: 2274: 2270: 2267:(1): 116–21. 2266: 2262: 2261: 2253: 2245: 2241: 2236: 2231: 2226: 2221: 2217: 2213: 2209: 2205: 2201: 2194: 2192: 2183: 2179: 2175: 2171: 2167: 2163: 2159: 2155: 2151: 2147: 2140: 2138: 2136: 2134: 2125: 2121: 2116: 2111: 2107: 2103: 2102:J. Biol. Chem 2099: 2092: 2090: 2081: 2077: 2073: 2069: 2065: 2061: 2057: 2053: 2049: 2042: 2034: 2030: 2026: 2022: 2015: 2007: 2003: 1998: 1993: 1990:(3): 225–29. 1989: 1985: 1978: 1971: 1969: 1964: 1956: 1954: 1949: 1944: 1942: 1938: 1934: 1924: 1922: 1919: 1915: 1914: 1909: 1905: 1904: 1899: 1889: 1887: 1883: 1880:tint made in 1879: 1875: 1871: 1867: 1863: 1859: 1855: 1854:personal care 1851: 1847: 1842: 1838: 1833: 1829: 1825: 1817: 1812: 1798: 1795: 1792: 1789: 1785: 1782: 1779: 1776: 1771: 1767: 1764: 1761: 1758: 1750: 1747: 1744: 1741: 1736: 1733: 1730: 1727: 1723: 1720: 1717: 1714: 1710: 1707: 1704: 1701: 1693: 1690: 1687: 1684: 1679: 1676: 1673: 1670: 1665: 1662: 1659: 1656: 1651: 1648: 1645: 1642: 1635: 1632: 1629: 1626: 1621: 1618: 1615: 1612: 1607: 1604: 1601: 1598: 1593: 1590: 1587: 1584: 1579: 1576: 1573: 1570: 1565: 1562: 1559: 1556: 1552: 1549: 1546: 1543: 1535: 1532: 1529: 1526: 1522: 1519: 1516: 1513: 1508: 1505: 1502: 1499: 1494: 1491: 1488: 1485: 1478: 1475: 1472: 1469: 1462: 1459: 1456: 1453: 1449: 1446: 1443: 1440: 1404: 1401: 1398: 1394: 1391: 1387: 1386:biotechnology 1383: 1380: 1376: 1372: 1369: 1365: 1362: 1358: 1355: 1352: 1348: 1344: 1340: 1337: 1336: 1331: 1327: 1323: 1322: 1316: 1313: 1309: 1300: 1291: 1289: 1278: 1276: 1271: 1262: 1259: 1258:Microfluidics 1253:Microfluidics 1250: 1242: 1234: 1232: 1228: 1222: 1214: 1202: 1199: 1196: 1193: 1189: 1186: 1183: 1180: 1177: 1173: 1170: 1167: 1164: 1161: 1157: 1153: 1151: 1150: 1145: 1142: 1139: 1136: 1133: 1130: 1129: 1124: 1121: 1118: 1115: 1112: 1110: 1107: 1106: 1103: 1100: 1097: 1094: 1090: 1087: 1083: 1082: 1075: 1061: 1056: 1047: 1039: 1027: 1024: 1021: 1018: 1015: 1012: 1011: 1010: 1008: 1007: 1001: 999: 991: 986: 983: 980:elongational 978: 975: 972: 968: 967: 963: 958: 951: 950: 949: 946: 944: 940: 930: 925: 915: 913: 909: 905: 899: 892: 891:garden spider 887: 873: 870: 869: 865: 862: 861: 857: 854: 853: 848: 845: 844: 840: 837: 836: 832: 829: 828: 823:Spider cocoon 821: 817: 815: 811: 807: 797: 794: 793: 789: 786: 785: 781: 778: 777: 773: 770: 769: 765: 763:Flagelliform 762: 761: 757: 754: 753: 749: 746: 745: 741: 738: 737: 734: 727: 726: 721: 717: 697: 696:Argiope picta 692: 679: 676: 673: 669: 666: 663: 659: 656: 651: 647: 644: 640: 637: 634: 630: 627: 624:forms a silk 623: 622: 617: 613: 612: 607: 604: 600: 597: 596: 592: 588: 585: 581: 578: 575: 572: 568: 565: 563:Reproduction 562: 558: 555: 551: 547: 543: 540: 536: 533: 529: 527:Prey capture 526: 521: 518: 515: 511: 502: 500: 496: 492: 487: 483: 473: 471: 467: 463: 459: 449: 440: 438: 434: 423: 421: 411: 409: 405: 401: 391: 389: 379: 369: 359: 357: 346: 344: 340: 336: 332: 328: 318: 316: 311: 302: 299: 297: 288: 284: 282: 278: 274: 270: 265: 249: 244: 243: 242: 237: 235: 231: 227: 223: 219: 214: 212: 208: 204: 200: 196: 192: 191:hydrogen ions 188: 184: 180: 176: 172: 168: 164: 160: 156: 152: 143: 129: 127: 123: 119: 114: 112: 106: 104: 100: 96: 92: 88: 84: 80: 76: 73: 69: 62: 58: 54: 50: 49: 48:Indian Summer 44: 37: 36: 30: 26: 22: 8026:Polyethylene 7800: 7453: 7236:. Retrieved 7231: 7216:. Retrieved 7212: 7199:Ghostarchive 7197:Archived at 7187:. Retrieved 7183: 7142: 7139:PLOS Biology 7138: 7100: 7091: 7081: 7048: 7044: 7041:Duarte F. J. 7035: 7023:. Retrieved 7017: 7011: 7003: 6998: 6963: 6959: 6949: 6935:(1): 37–41. 6932: 6928: 6922: 6914: 6909: 6876: 6872: 6866: 6857: 6847: 6835:. Retrieved 6831: 6822: 6787: 6783: 6773: 6765:the Guardian 6764: 6754: 6729: 6725: 6719: 6689:(1): 31–38. 6686: 6682: 6676: 6651: 6648:Biochemistry 6647: 6637: 6610: 6604: 6594: 6561: 6557: 6551: 6510: 6506: 6500: 6483: 6479: 6473: 6448: 6444: 6438: 6413: 6409: 6403: 6378: 6374: 6368: 6351: 6347: 6341: 6316: 6312: 6306: 6271: 6265: 6255: 6222: 6218: 6212: 6203: 6199: 6193: 6148: 6144: 6134: 6109: 6105: 6098: 6089: 6083: 6058: 6054: 6048: 6036:. Retrieved 6032: 6022: 6013: 6003: 5989: 5952: 5948: 5938: 5913: 5907: 5901: 5889:. Retrieved 5885:the original 5871: 5859:. Retrieved 5855:the original 5841: 5827: 5813: 5801:. Retrieved 5791: 5738: 5734: 5728: 5720: 5708:. Retrieved 5653: 5649: 5639: 5620: 5616: 5606: 5565: 5561: 5536:(3): 80–86. 5533: 5530:Mater. Today 5529: 5519: 5505: 5460: 5456: 5446: 5411: 5407: 5397: 5363: 5359: 5349: 5323: 5319: 5312: 5277: 5273: 5263: 5222: 5218: 5212: 5167: 5163: 5153: 5128: 5124: 5117: 5092: 5088: 5037: 5033: 4990: 4986: 4980: 4961: 4928: 4924: 4918: 4875: 4871: 4829: 4825: 4819: 4776: 4772: 4762: 4748:cite journal 4715: 4711: 4698: 4673: 4669: 4663: 4637:10.3791/2382 4631:(47): 2382. 4628: 4618: 4585: 4581: 4575: 4566: 4562: 4556: 4547: 4543: 4537: 4512: 4508: 4450: 4446: 4440: 4415: 4411: 4405: 4380: 4376: 4370: 4345: 4341: 4335: 4310: 4306: 4300: 4273: 4269: 4259: 4224: 4220: 4210: 4173: 4169: 4159: 4134: 4130: 4124: 4099: 4095: 4089: 4046: 4042: 4032: 4007: 4003: 3953: 3949: 3905: 3901: 3891: 3875:(3): 80–86. 3872: 3869:Mater. Today 3868: 3858: 3823: 3819: 3779: 3775: 3734:(1): 50–56. 3731: 3727: 3721: 3702: 3698: 3648: 3644: 3598: 3594: 3588: 3571: 3568:Science News 3567: 3561: 3524: 3497: 3491: 3472: 3436: 3432: 3426: 3401: 3351: 3347: 3337: 3302: 3298: 3234:(9): 11234. 3231: 3227: 3184:(1): 84–88. 3181: 3177: 3171: 3159:. Retrieved 3149: 3108: 3104: 3054: 3050: 2996: 2992: 2982: 2970:. Retrieved 2966:the original 2955: 2943:. Retrieved 2941:. matweb.com 2933: 2921:. Retrieved 2919:. matweb.com 2911: 2878: 2874: 2868: 2833: 2829: 2819: 2794: 2790: 2780: 2729: 2725: 2682: 2678: 2635:(1): 25–30. 2632: 2626: 2574: 2570: 2564: 2539: 2535: 2525: 2500: 2496: 2490: 2441:(10): e998. 2438: 2434: 2424: 2391: 2385: 2379: 2354: 2350: 2333: 2300: 2295: 2289: 2264: 2258: 2252: 2207: 2203: 2149: 2145: 2105: 2101: 2055: 2051: 2041: 2024: 2020: 2014: 1987: 1983: 1945: 1930: 1911: 1901: 1895: 1846:mass-produce 1843: 1821: 1769: 1342: 1333: 1329: 1311: 1305: 1287: 1284: 1281:Other shapes 1268: 1256: 1248: 1240: 1223: 1220: 1212: 1159: 1147: 1126: 1108: 1092: 1085: 1053: 1044: 1004: 1002: 995: 990:helical pump 982:shear stress 947: 936: 900: 896: 803: 731: 723: 695: 664:Alarm lines 655:Paramystaria 654: 635:Guide lines 619: 609: 593: 508: 501:enclosures. 495:microfibrils 479: 469: 461: 455: 446: 429: 419: 417: 407: 397: 385: 365: 352: 342: 324: 314: 308: 300: 293: 266: 263: 238: 218:crystallites 215: 148: 115: 107: 67: 66: 46: 33: 25: 7857:Regenerated 7801:Spider silk 7490:Spider bite 7444:Palpal bulb 7434:Opisthosoma 7399:Calamistrum 7304:Cannibalism 7286:Arachnology 7051:(3): 5710. 6790:(1): 8–23. 6507:Soft Matter 5710:26 November 5513:(in German) 4221:Nat. Commun 3820:Biopolymers 3651:(8): 1290. 3299:Soft Matter 2797:: 227–243. 2536:Soft Matter 2503:(20): 623. 2027:(1): 1–10. 1913:N. clavipes 1835: [ 1830:missionary 1660:Termonia, Y 1343:N. clavipes 1275:Taylor cone 1128:Bombyx mori 771:Tubuliform 716:Crab spider 626:diving bell 437:plasticiser 426:Temperature 376:10 J/m 240:stretching. 183:hygroscopic 179:Pyrrolidine 175:beta sheets 68:Spider silk 8121:Polyamides 8105:Categories 8006:Modacrylic 8001:Microfiber 7918:Triacetate 7870:Milk fiber 7736:Camel hair 7668:Lotus silk 7511:Spider web 7409:Chelicerae 7351:Mesothelae 7294:Ballooning 6061:: 92–102. 6038:8 February 5803:15 October 5562:Adv. Mater 4043:Biophys. 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