Collagen evolution of collagens was a fundamental step in the early evolution of life, supporting the coalescence of multicellular life forms. Collagen D-banding is viable as periodic formation of ridging on all fibrils forming collagen. D-bands are created due to the semi-crystalline formation of the collagen within the fibrils. The pattern exhibited by D-banding is consistently independent of fibril diameter. When undergoing deformation, collagen fibrils may lose their D-banding, making the disappearance of the d-bands an indicator of the type of damage undergone by then tendon fibrils. Collagen Collagen is the main structural protein in the extracellular space in the various
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