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In molecular biology, fibrous proteins or scleroproteins are one of the three main classifications of protein structure (alongside globular and membrane proteins). [1] Fibrous proteins are made up of elongated or fibrous polypeptide chains which form filamentous and sheet-like structures. This kind of protein can be distinguished from globular ...
Elastin is a fibrous protein common in various soft tissues, like skin, blood vessels and lung tissue. Each monomer connects with each other, forming a 3D network, with ability to endure over 200% strain before deformation. [13] Keratin is a structural protein mainly found in hair, nails, hooves, horns, quills. [14]
Connective tissue is found in between other tissues everywhere in the body, including the nervous system. The three meninges, membranes that envelop the brain and spinal cord, are composed of connective tissue. Most types of connective tissue consists of three main components: elastic and collagen fibers, ground substance, and cells. [2]
Structural proteins confer stiffness and rigidity to otherwise-fluid biological components. Most structural proteins are fibrous proteins; for example, collagen and elastin are critical components of connective tissue such as cartilage, and keratin is found in hard or filamentous structures such as hair, nails, feathers, hooves, and some animal ...
The collagen protein is composed of a triple helix, which generally consists of two identical chains (α1) and an additional chain that differs slightly in its chemical composition (α2). [23] The amino acid composition of collagen is atypical for proteins, particularly with respect to its high hydroxyproline content.
Maintenance of crosslinked elastin is carried out by a number of proteins including lysyl oxidase-like 1 protein. [ 13 ] Mature elastic fibers consist of an amorphous elastin core surrounded by a glycosaminoglycans, heparan sulphate, [ 14 ] and number of other proteins such as microfibrillar-associated glycoproteins , fibrillin , fibullin , and ...
The heavy fibroin protein consists of layers of antiparallel beta sheets. Its primary structure mainly consists of the recurrent amino acid sequence ( Gly - Ser -Gly- Ala -Gly-Ala) n . The high glycine (and, to a lesser extent, alanine) content allows for tight packing of the sheets, which contributes to silk's rigid structure and tensile strength.
Further investigations found evidence that supports that all IF proteins arose from a common lamin-like ancestor. This theory is based on the observation that organisms that contain IF proteins necessarily contain lamins as well; however, the presence of lamins is not a requirement for simultaneously containing IF proteins.