Myosin with two FERM domains in the tail region. It has an extended lever arm consisting of five calmodulin binding IQ motifs followed by a single alpha helix (SAH). Myosin VII is required for phagocytosis in "Dictyostelium discoideum", spermatogenesis in "C. elegans" and stereocilia formation in mice and zebrafish. Myosin VIII is a plant-specific myosin linked to cell division; specifically, it is involved in regulating the flow of cytoplasm between cells and in the localization of vesicles to the phragmoplast. Myosin IX is a group of single-headed motor proteins. It was first shown to be minus-end directed, but a later study
Elastin-like polypeptides oxidase. One of the major reasons that elastin can withstand high levels of stress in the body without experiencing any physical deformation is that the underlying tropoelastin contains domains that are highly hydrophobic. These hydrophobic domains, consisting overwhelmingly of alanine, proline, glycine, and valine, tend towards instability and disorderliness, ensuring that the elastin does not lock into any specific confirmation. Thus, ELPs consisting of the Val-Pro-Gly-X-Gly monomeric units, which bear resemblance to the repetitive tropoelastin hydrophobic domains, are highly disordered below their T Even above their T in their aggregated state, ELPs are only partially ordered. This is due to