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Keratin is a crucial fibrous protein found in animals, constituting tough structures like hair, feathers, nails, and horns. It's classified based on tissue origin and sulfur content: soft keratins have lower sulfur, while hard keratins, found in hair and claws, contain more sulfur, creating a stronger structure. [2]
Keratin (/ ˈ k ɛr ə t ɪ n / [1] [2]) is one of a family of structural fibrous proteins also known as scleroproteins. Alpha-keratin (α-keratin) is a type of keratin found in vertebrates. It is the key structural material making up scales, hair, nails, feathers, horns, claws, hooves, and the outer layer of skin among vertebrates.
Keratin-associated proteins (KRTAPs, KAPs) and keratins are the major components of hair and nails. The content of KRTAPs in hair varies considerably between species, ranging from less than 3% in human hair to 30–40% in echidna quill. Both keratin and KRTAPs are extensively cross-linked in hair through disulfide bonds via numerous cysteine ...
Nails are a distinguishing feature of the primate order. The nail is an unguis, meaning a keratin structure at the end of a digit. Other examples of ungues include the claw, hoof, and talon. The nails of primates and the hooves of running mammals evolved from the claws of earlier animals. [38]
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.
In humans, some of the more common skin appendages are hairs (sensation, heat loss, filter for breathing, protection), arrector pilli (smooth muscles that pull hairs straight), sebaceous glands (secrete sebum onto hair follicle, which oils the hair), sweat glands (can secrete sweat with strong odour or with a faint odour (merocrine or eccrine ...
Keratin is a structural protein mainly found in hair, nails, hooves, horns, quills. [14] Basically keratin is formed by polypeptide chains, which coil into α-helices with sulfur cross-links or bond into β-sheets linked by hydrogen bonding. β-keratin, which is tougher than α-conformation, is more common in birds and reptiles.
The hair cuticle is also known to contain anteiso-18-methyleicosanoic acid which contribute to the hydrophobic properties of hair. [5] [4] Diagram of the hair shaft, indicating medulla (innermost), cortex, and cuticle (exterior) While the cuticle is the outermost layer, it is not responsible for the color of the hair.