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This source came from new scientist, article was written by "book club" it is a very informative new discovery. A spider tread carries a neutron this is a liquid its flowing naturally and carries structural properties for example a natural gluing effect. Its composite bio polymer structure includes different proteins which form so-called nano-fibrils, which consist of alternating nanometre-sized crystalline structures and semi-amorphous regions. The nano-fibrils are themselves embedded in an amorphous matrix. The crystals reinforce the fibre while the amorphous region gives extensibility and transfers load between the nano-fibrils. The silk precursor proteins’ behaviour is completely counter intuitive. Native concentration inside the worm can be up to 400mg/ml. “This is an extraordinarily high concentration for the proteins to remain "stably dispersed throughout the solution” Book Club ascertained from Dr Cedric Dicko, a French biochemist working both in England and Sweden. “Even stranger, as the concentration drops the proteins begin to "expand and flow" until "they eventually clump together – this is the reverse of what we’d expected.”Also at the native concentration the proteins form a compact helical structure with a radius of gyration of about 90nm; as they are diluted they unfold until they are 130nm in size. In the lab, the effect is a like a neat ball of string becoming unravelled into a big mess that ties itself in knots. However, the silkworms are able to control this process so that the proteins are spun into highly ordered silk filaments as they unfold and begin to flow. Although Silk may be six times stronger than steel by weight, but it is its toughness that makes it so special. The threads which make up these remarkable structures are bio polymers. But before we can produce and use artificial spider silk, we need to understand what gives it its unique mechanical properties. Many different research fields are interested in spider silk. The structure of native silk fibrin at near in Vito conditions. Comparing native and reconstituted silk we observed significant differences in sizes, molecular weights, refolding and interactions. These observations question the validity of a presently widespread approach in silk analysis. An alcogel was elucidated from morphological observations using TEM, AFM and confocal laser scanning microscopy (CLSM) as well as the kinetic studies by Thioflavin T fluorescence and rheological methods. An intriguing dual-structure—a nanofibrillar network on the nanoscale and a floc-like network on the micro scale—was observed within the RSF alcogel. Based on our kinetic study, the fractal dimension of the ramified fibular aggregate was found to be 2.4–2.8 depending on RSF concentration. Meanwhile, through a scaling analysis of the mechanical properties of RSF alcogels, the fractal dimension of the floc-linked network was also found. Note here there is a protein that carries electron orbitals with a faction neutron it like a wound coil spring with an equation that equal to it the "sprung" Researchers envisage using a copy of this polymer as a medical suture or in ligament repair, because it does not tire when frequently flexed and can withstand regular impact and great pressure. The military sector is also interested in this material because its ability to dissipate energy could make it ideal for lightweight armour. The new observations by the Oxford/Lund team allow the "regenerated proteins to be compared with the native precursors and it finally gives a benchmark,”