An emerging class of disordered proteins underlies the elasticity of many biological tissues. Elastomeric proteins are essential to the function of biological machinery as diverse as the human arterial wall, the capture spiral of spider webs and the jumping mechanism of fleas. In this chapter, we review what is known about the molecular basis and the functional role of structural disorder in protein elasticity. In general, the elastic recoil of proteins is due to a combination of internal energy and entropy. In rubber‑like elastomeric proteins, the dominant driving force is the increased entropy of the relaxed state relative to the stretched state. Aggregates of these proteins are intrinsically disordered or fuzzy, with high polypeptide chain entropy. We focus our discussion on the sequence, structure and function of five rubber‑like elastomeric proteins, elastin, resilin, spider silk, abductin and ColP. Although we group these disordered elastomers together into one class of proteins, they exhibit a broad range of sequence motifs, mechanical properties and biological functions. Understanding how sequence modulates both disorder and elasticity will help advance the rational design of elastic biomaterials such as artificial skin and vascular grafts.