Scleroprotein these can form unusual secondary structures, such as a collagen helix. The structures often feature cross-links between chains (e.g., cys-cys disulfide bonds between keratin chains). Scleroproteins tend not to denature as easily as globular proteins. Miroshnikov et al. (1998) are among the researchers who have attempted to synthesize fibrous proteins. 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
Myosin cells, the long coiled-coil tails of the individual myosin molecules join together, forming the thick filaments of the sarcomere. The force-producing head domains stick out from the side of the thick filament, ready to walk along the adjacent actin-based thin filaments in response to the proper chemical signals. Myosin III is a poorly understood member of the myosin family. It has been studied "in vivo" in the eyes of "Drosophila", where it is thought to play a role in phototransduction. A human homologue gene for myosin III, MYO3A, has been uncovered through the Human Genome Project and is expressed in