Alpha-keratin Alpha-keratin Alpha-keratin, or α-keratin, is a type of keratin found in mammals. This protein is the primary component in hairs, horns, 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. The secondary structure of α-keratin is very similar to that of a traditional protein α-helix and forms a coiled coil. Due to its tightly wound structure, it can function as one of the strongest biological materials and has various uses in mammals, from predatory claws to hair for warmth. α-keratin is
Translocase of the outer membrane internal targeting signals, not all of which have been identified, and include proteins that take on a β-barrel structure, such as Tom40. Some proteins however, that are targeted to the outer mitochondrial membrane contain a hydrophobic tail domain that anchors the protein to the membrane. The translocase of the outer membrane (TOM) forms a complex made of Tom70, Tom22, and Tom20, along with Tom40, Tom7, Tom6, and Tom5. Tom20 and Tom22 are preprotein receptors, which are responsible for recognition of the cleavable presequence possessed by mitochondrial-targeted proteins. Tom70 is also a preprotein receptor and may recognise some cleavable presequence proteins,