Scleroprotein Scleroprotein Scleroproteins or fibrous proteins constitute one of the three main types of proteins (alongside globular and membrane proteins). There are many scleroprotein superfamilies including keratin, collagen, elastin, and fibroin. The roles of such proteins include protection and support, forming connective tissue, tendons, bone matrices, and muscle fiber. A scleroprotein forms long protein filaments, which are shaped like rods or wires. Scleroproteins are structural proteins or storage proteins that are typically inert and water-insoluble. A scleroprotein occurs as an aggregate due to hydrophobic side chains that protrude from the molecule. A scleroprotein's peptide sequence often has limited residues with repeats;
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