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
Major basic protein MBP does not bind either calcium or any of the other carbohydrates that this family recognize. Instead, MBP recognises heparan sulfate proteoglycans. Two crystallographic structures of MBP have been determined. Major basic protein has been shown to interact with Pregnancy-associated plasma protein A. arylsulfatase Major basic protein Eosinophil Major basic protein, often shortened to Major basic protein (MBP) (also called Proteoglycan 2(PRG2)) in humans is encoded by the "PRG2" gene. The protein encoded by this gene is the predominant constituent of the crystalline core of the eosinophil granule. High levels of the proform of this protein are also present in