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 head although some forms have a globular region in their C-terminal. There are many cell-specific isoforms of myosin heavy chains, coded for by a multi-gene family. Myosin interacts with actin to convert chemical energy, in the form of ATP, to mechanical energy. The 3-D structure of the head portion of myosin has been determined and a model for actin-myosin complex has been constructed. The globular head is well conserved, and is key to contraction. Muscle contraction results from an attachment–detachment cycle between the myosin heads extending from myosin filaments and the sites on actin filaments. The myosin head first attaches to