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
HspQ protein domain could occurs through binding of YccV itself to fully or hemimethylated DNA. In addition, studies have identified the "yccV" gene as one of three insertion sites in mini-Tn10 which suppress dnaA46 thermosensitivity. This protein domain is thought to have a SH3-like barrel structure. Additionally, the structure of a hypothetical protein in this family has been solved and it forms a beta sheet structure with a terminating alpha helix. HspQ forms a stable homodimer in solution and can form homomultimers consisting of about four monomers. The theoretical molecular mass of the HspQ protein were calculated to be 11.8 kDa. It is