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Dragline silk fiber was originally thought to be made up of two types of spidroins, spidroin-1 (MaSp1) and spidroin-2 (MaSp2) however recent transcriptomic analysis of over 1000 spider species has revealed multiple spidroins are expressed making it much more complex. [2] [3] [4] Spidroin is part of a large group of proteins called scleroproteins.
Animal fibers are natural fibers that consist largely of certain proteins. Examples include silk, hair/fur (including wool) and feathers. The animal fibers used most commonly both in the manufacturing world as well as by the hand spinners are wool from domestic sheep and silk. Also very popular are alpaca fiber and mohair from Angora goats.
Fibroin is an insoluble protein present in silk produced by numerous insects, such as the larvae of Bombyx mori, and other moth genera such as Antheraea, Cricula, Samia and Gonometa. 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.
Kinesin is a protein functioning as a molecular biological machine. It uses protein domain dynamics on nanoscales. A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. Protein complexes are distinct from multidomain enzymes, in which multiple catalytic domains are found in a single polypeptide chain ...
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.
Spider silk structure: crystalline beta-sheets separated by amorphous linkages. Silks have a hierarchical structure. The primary structure is the amino acid sequence of its proteins (), mainly consisting of highly repetitive glycine and alanine blocks, [4] [5] which is why silks are often referred to as a block co-polymer.
A representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).
He called this protein myosin. [ 3 ] [ 4 ] The term has been extended to include a group of similar ATPases found in the cells of both striated muscle tissue and smooth muscle tissue . Following the discovery in 1973 of enzymes with myosin-like function in Acanthamoeba castellanii , a global range of divergent myosin genes have been discovered ...