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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.
Cell junctions are especially abundant in epithelial tissues. Combined with cell adhesion molecules and extracellular matrix, cell junctions help hold animal cells together. Cell junctions are also especially important in enabling communication between neighboring cells via specialized protein complexes called communicating (gap) junctions ...
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 ...
The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including those of bacteria and archaea. [2] In eukaryotes , it extends from the cell nucleus to the cell membrane and is composed of similar proteins in the various organisms.
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.
The proteins are called connexins. Gap junction proteins include the more than 26 types of connexin, and at least 12 non-connexin components that make up the gap junction complex or nexus. [4] These components include the tight junction protein ZO-1—a protein that holds membrane content together and adds structural clarity to a cell, [5 ...
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.
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 ...