Alpha-keratin higher level of force before fracture. On the other hand, soft alpha-keratins, such as ones found in the skin, contain a comparatively smaller amount of disulfide bonds, making their structure more flexible. 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
Virulence-related outer membrane protein family invasion and helps defend against the complement system. Although OmpX has the same beta-sheet topology as the structurally related outer membrane protein A (OmpA) , their barrels differ with respect to the shear numbers and internal hydrogen-bonding networks. OspA from Borrelia burgdorferi is an unusual outer surface protein, it has two globular domains which are connected with a single-layer β-sheet. This protein is highly soluble, contains a large number of Lys and Glu residues. These high entropy residues may disfavor crystal packing. Virulence-related outer membrane protein family Virulence-related outer membrane proteins are expressed in Gram-negative bacteria and are essential to