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
Myosin like a dynamic tether, retaining vesicles and organelles in the actin-rich periphery of cells. A recent single molecule in vitro reconstitution study on assembling actin filaments suggests that Myosin V travels farther on newly assembling (ADP-Pi rich) F-actin, while processive runlengths are shorter on older (ADP-rich) F-actin. Myosin VI is an unconventional myosin motor, which is primarily processive as a dimer, but also acts as a nonprocessive monomer. It walks along actin filaments, travelling towards the pointed end (- end) of the filaments. Myosin VI is thought to transport endocytic vesicles into the cell. Myosin VII is an unconventional myosin