Keratin 5 Keratin 5 Keratin 5, also known as KRT5, K5, or CK5, is a protein that is encoded in humans by the "KRT5" gene. It dimerizes with keratin 14 and forms the intermediate filaments (IF) that make up the cytoskeleton of basal epithelial cells. This protein is involved in several diseases including epidermolysis bullosa simplex and breast and lung cancers. Keratin 5, like other members of the keratin family, is an intermediate filament protein. These polypeptides are characterized by a 310 residue central rod domain that consists of four alpha helix segments (helix 1A, 1B, 2A, and 2B) connected by three
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