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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 protein by its low solubility in water. In contrast, globular proteins are spherical and generally soluble in water, performing dynamic functions like enzymatic ...
Collagen is one of the long, fibrous structural proteins whose functions are quite different from those of globular proteins, such as enzymes. Tough bundles of collagen called collagen fibers are a major component of the extracellular matrix that supports most tissues and gives cells structure from the outside, but collagen is also found inside ...
Silk in its raw state consists of two main proteins, sericin and fibroin, with a glue-like layer of sericin coating two singular filaments of fibroin called brins. [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
Three-dimensional structure [1] of an alpha helix in the protein crambin. An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure, and it is ...
Items that fit into the Mediterranean diet can be found at Subway, Chick-fil-A, Wendy's, and others. Often, the start of the new year can mark the start of new diet plans.
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 molecular biology, the collagen triple helix or type-2 helix is the main secondary structure of various types of fibrous collagen, including type I collagen. In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data.
The connective tissue protein elastin also has a high percentage of both glycine and alanine. Silk fibroin, considered a β-keratin, can have these two as 75–80% of the total, with 10–15% serine, with the rest having bulky side groups. The chains are antiparallel, with an alternating C → N orientation. [22]