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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 shells.
This can be done in terms of the chemical elements present, or by molecular structure e.g., water, protein, fats (or lipids), hydroxyapatite (in bones), carbohydrates (such as glycogen and glucose) and DNA. In terms of tissue type, the body may be analyzed into water, fat, connective tissue, muscle, bone, etc.
Collagen (/ ˈ k ɒ l ə dʒ ə n /) is the main structural protein in the extracellular matrix of the connective tissues of many animals. It is the most abundant protein in mammals, [1] making up 25% to 35% of protein content. Amino acids are bound together to form a triple helix of elongated fibril [2] known as a collagen helix.
At the top level are all alpha proteins (domains consisting of alpha helices), all beta proteins (domains consisting of beta sheets), and mixed alpha helix/beta sheet proteins. While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred to as metamorphic proteins. [5]
Protein is a nutrient needed by the human body for growth and maintenance. Aside from water, proteins are the most abundant kind of molecules in the body. Protein can be found in all cells of the body and is the major structural component of all cells in the body, especially muscle. This also includes body organs, hair and skin.
A protein structure database is a database that is modeled around the various experimentally determined protein structures. The aim of most protein structure databases is to organize and annotate the protein structures, providing the biological community access to the experimental data in a useful way.
Ferritin is found in most tissues as a cytosolic protein, but small amounts are secreted into the serum where it functions as an iron carrier. Plasma ferritin is also an indirect marker of the total amount of iron stored in the body; hence, serum ferritin is used as a diagnostic test for iron-deficiency anemia and iron overload. [4]
The major force that keeps the coiled-coil structure is hydrophobic interactions between apolar residues along the keratin's helical segments. [21] Limited interior space is the reason why the triple helix of the (unrelated) structural protein collagen, found in skin, cartilage and bone, likewise has a high percentage of glycine.