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Coil zipper—also known as nylon coil zipper—is a type of zipper whose teeth/elements are made from coiled monofilament that is traditionally nylon. The coil zipper was first invented in 1940, however not commonly used until the 1960's. [1] [2] The coil is sewn to a zipper tape to make the final product. The final zipper product is completed ...
Coil zippers are made of polyester coil and are thus also termed polyester zippers. Nylon was formerly used to make them, and though only polyester is used now, [citation needed] the type is still also termed a nylon zipper. Invisible zippers have the teeth hidden behind a tape, so that the zipper is invisible. It is also called the concealed ...
A major technological change came in 1950, when the company purchased a chain machine from the U.S. that allowed the automation of the zipper making process. Previously, YKK zippers were made by hand, and hence had an inferior quality compared to automated zippers from abroad. In March 1951, YKK relocated its headquarters to Chūō, Tokyo.
Nylon is a family of synthetic polymers characterized by amide linkages, typically connecting aliphatic or semi-aromatic groups.. Nylons are generally white or colorless [1] [failed verification] [2] [failed verification] and possess a soft texture, with some varieties exhibiting a silk-like appearance.
Unlike an invisible zipper where the coil is also on the back, the reverse coil shows stitching on the front side and the slider will accommodate a variety of pulls (the invisible zipper requires a small, tear-drop pull due to the small slider attachment).
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The Goodrich company registered the trademark name Zipper in 1943, so that no other company could legally use the name, though individuals informally referred to slide fasteners as zippers. The trademark expired in 1986 and was not renewed, so it is now legal for other companies to call their products zippers. [7] [8]
A coiled coil is a structural motif in proteins in which 2–7 [1] alpha-helices are coiled together like the strands of a rope. (Dimers and trimers are the most common types.) They have been found in roughly 5-10% of proteins and have a variety of functions. [2] They are one of the most widespread motifs found in protein-protein interactions.
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