Beta-keratin 75-80% of the amino acids in silk, another 10-15% is serine and the final 10% contain bulky side chains such as in tyr, arg, val, asp, and glu. Beta-keratin β-keratin or beta-keratin is a member of a structural protein family found in the epidermis of reptiles and birds . β-keratins were named so because they are components of epidermal stratum corneum rich in stacked β pleated sheets, in contrast to alpha-keratins, intermediate-filament proteins also found in stratum corneum and rich in alpha helices. Because the accurate use of the term "keratin" is limited to the alpha-keratins, the term "beta-keratins" in
Elastin glycine and proline, which form mobile hydrophobic regions bounded by crosslinks between lysine residues. Multiple transcript variants encoding different isoforms have been found for this gene. Elastin's soluble precursor is tropoelastin. The characterization of disorder is consistent with an entropy-driven mechanism of elastic recoil. It is concluded that conformational disorder is a constitutive feature of elastin structure and function. Deletions and mutations in this gene are associated with supravalvular aortic stenosis (SVAS) and the autosomal dominant cutis laxa. Other associated defects in elastin include Marfan syndrome, emphysema caused by α-antitrypsin deficiency, atherosclerosis, Buschke-Ollendorff syndrome, Menkes syndrome, pseudoxanthoma elasticum, and Williams