Silk is an externally spun fibrous protein secretion formed into fibers, usually resulting in material structures such as cocoons or webs [1-4]. Silks are essentially pure proteins, with only in some Of all the natural silks represent the only ones that are spun. Silk fibers from silkworms have been used in textiles for nearly 5000 years. The primary reasons for this longtime use have been the unique luster, tactile properties, durability, and dyability of silks. Silk fibers are remarkable materials displaying unusual mechanical properties: strong, extensible, and mechanically compressible. Silks also display interesting thermal and electromagnetic responses, particularly in the UV range for insect entrapment and form crystalline phases related to processing. Silk fibers were used in optical instruments as late as the mid-1900s because of their fine and uniform diameter and high strength and stability over a range of temperatures and humidity. Naturalist reports suggest that some spider silks were used in the South Pacific for gill nets, dip nets, and fishing-a testimony to the remarkable mechanical properties and durability of this family of protein polymers. Silks have historically been used in medicine as sutures over the past 100 years and are currently used today in this mode along with a variety of consumer product applications. Commercially, silkworm cocoons are mass produced in a process termed ‘‘sericulture’’. The cocoons are extracted in hot soapy water to remove the sericin gluelike protein. The remaining fibroin or structural silk is reeled onto spools, yielding approximately 300-1200 m of usable thread per cocoon. These threads can be dyed or modified for textile applications. The annual world production of raw silk is about 60,000 tons, with China producing half of the world supply followed by India, Korea, and Japan. Silks represent one member of a larger class of fibrous proteins in nature, which include keratins, collagens, elastins, and others [5]. These types of proteins can be considered nature’s equivalent of synthetic block copolymers. Aside from their direct use in materials applications, fibrous proteins provide experimentally accessible model systems with simpler and well-controlled genetic template-based protein synthesis. The highly repetitive structure allows key features of the primary sequences of these proteins to be captured in shorter consensus sequences at the corresponding genetic level. Short synthetic genetic variants can then be combined to generate larger genes and thus proteins that represent mimics of the native protein. This technique is useful in simplifying the complex behavior of these proteins to an intelligible level, while retaining their biological relevance and materials function. These shorter genetic variants, when polymerized (multimerized) into longer genes, can be used to explore protein sequence and size relationships.