Keratin (genitive ') meaning "horn" originating from the Proto-Indo-European "*ḱer-" of the same meaning. It is composed of "horn like", i.e., kerato, to which the chemical suffix -in is appended. The Greek ' is used in many animal names, e.g. "Rhinoceros", meaning "nose with a horn". Keratin filaments are abundant in keratinocytes in the cornified layer of the epidermis; these are proteins which have undergone keratinization. In addition, keratin filaments are present in epithelial cells in general. For example, mouse thymic epithelial cells (TECs) are known to react with antibodies for keratin 5, keratin 8, and keratin 14. These antibodies are
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