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Sericin is composed of 18 different amino acids, of which 32% is serine.The secondary structure is usually a random coil, but it can also be easily converted into a β-sheet conformation, via repeated moisture absorption and mechanical stretching.
[1] [2] [3] Silk fibroin is considered a β-keratin related to proteins that form hair, skin, nails and connective tissues. Primary structure of fibroin, (Gly-Ser-Gly-Ala-Gly-Ala) n. The silk worm produces fibroin with three chains, the light, heavy, and the glycoprotein P25.
Keratin (/ ˈ k ɛr ə t ɪ n / [1] [2]) is one of a family of structural fibrous proteins also known as scleroproteins. It is the key structural material making up scales , hair , nails , feathers , horns , claws , hooves , and the outer layer of skin in vertebrates.
Keratin is a structural protein located at the hard surfaces in many vertebrates. Keratin has two forms, α-keratin and β-keratin , that are found in different classes of chordates. The naming convention for these keratins follows that for protein structures: alpha keratin is helical and beta keratin is sheet-like.
Keratohyalin is a protein structure found in cytoplasmic granules of the keratinocytes in the stratum granulosum of the epidermis.Keratohyalin granules (KHG) mainly consist of keratin, profilaggrin, [1] loricrin [2] and trichohyalin proteins which contribute to cornification or keratinization, the process of the formation of epidermal cornified cell envelope.
Alpha-keratin, or α-keratin, is a type of keratin found in mammalian vertebrates. This protein is the primary component in hairs , horns , claws , nails and the epidermis layer of the skin . α-keratin is a fibrous structural protein , meaning it is made up of amino acids that form a repeating secondary structure.
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