Protein fold class fixed or ordered three-dimensional structure. IDPs cover a spectrum of states from fully unstructured to partially structured and include random coils, (pre-)molten globules, and large multi-domain proteins connected by flexible linkers. They constitute one of the main types of protein (alongside globular, fibrous and membrane proteins). Coiled coil proteins form long, insoluble fibers involved in the extracellular matrix. There are many scleroprotein superfamilies including keratin, collagen, elastin, and fibroin. The roles of such proteins include protection and support, forming connective tissue, tendons, bone matrices, and muscle fiber. Small proteins typically have little secondary structure and often contain multiple disulphide bonds.
Beta-keratin whose flight capabilities have been questioned, would have had avian, but not feather, β-keratins. The small alvarezsaurid dinosaur "Shuvuuia deserti" shows evidence of a featherlike skin covering. Analysis by Schweitzer "et al." (1999) showed that these featherlike structures consisted of beta-keratin. There are two main forms of keratin, alpha-keratin and beta-keratin. Alpha-keratin is seen in humans and other mammals, beta-keratin is present in birds and reptiles. Beta-keratin is harder than alpha-keratin. Structurally alpha-keratin have alpha-helical coiled coil structure while beta-keratin have twisted beta sheet structure.bIn the case of β-sheets, this allows sterically-unhindered hydrogen bonding between the amino and carboxyl groups