Fibroin is a fibrillar protein excreted by silkworms.
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Fibroin is a protein, the building material of silk fibers. Silk is formed from the secretion of the pupating silkworm as it feeds on the leaves of mulberry trees. Fibroin belongs to the group of fibrillar proteins, which have long, string-like molecules.
The structure of their polypeptide chain can only be an alpha-helix or a beta-sheet.
The conformation of fibroin has a beta-sheet structure: polypeptide chains are arranged parallel to each other and form pleated sheets. The structure is stabilized by hydrogen bonds between the chains.
Fibroin cannot be dissolved in ordinary solvents but dissolves in concentrated alkaline solutions, copper-oxide ammonia and zinc-chloride.
Typical silk types include damask, organza, satin and taffeta.
While the density of spider silk is less than that of nylon filaments, its tensile strength is greater than that of steel.
Amino acids are the monomers of proteins.
Oxygen carrier protein in our red blood cells.
Polypeptide chains are composed of amino acids and can appear in alpha-helix or beta-sheet form.
The structure and arrangement of polypeptide chains affects the spatial structure of proteins.
Carrier of genetic information in cells.