Beta-keratin 75-80% of the amino acids in silk, another 10-15% is serine and the final 10% contain bulky side chains such as in tyr, arg, val, asp, and glu. Beta-keratin β-keratin or beta-keratin is a member of a structural protein family found in the epidermis of reptiles and birds . β-keratins were named so because they are components of epidermal stratum corneum rich in stacked β pleated sheets, in contrast to alpha-keratins, intermediate-filament proteins also found in stratum corneum and rich in alpha helices. Because the accurate use of the term "keratin" is limited to the alpha-keratins, the term "beta-keratins" in
Myosin showed that it is plus-end directed. The movement mechanism for this myosin is poorly understood. Myosin X is an unconventional myosin motor, which is functional as a dimer. The dimerization of myosin X is thought to be antiparallel. This behavior has not been observed in other myosins. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments. Some research suggests it preferentially walks on bundles of actin, rather than single filaments. It is the first myosin motor found to exhibit this behavior. Myosin XI directs the movement of organelles such