The passive elasticity of muscle is largely governed by the I-band part of the giant muscle protein titin1, 2, 3, 4, a complex molecular spring composed of a series of individually folded immunoglobulin-like domains as well as largely unstructured unique sequences5. These mechanical elements have distinct mechanical properties, and when combined, they provide the desired passive elastic properties of muscle6, 7, 8, 9, 10, 11, which are a unique combination of strength, extensibility and resilience. Single-molecule atomic force microscopy (AFM) studies demonstrated that the macroscopic behaviour of titin in intact myofibrils can be reconstituted by combining the mechanical properties of these mechanical elements measured at the single-molecule level8. Here we report artificial elastomeric proteins that mimic the molecular architecture of titin through the combination of well-characterized protein domains GB112 and resilin13. We show that these artificial elastomeric proteins can be photochemically crosslinked and cast into solid biomaterials. These biomaterials behave as rubber-like materials showing high resilience at low strain and as shock-absorber-like materials at high strain by effectively dissipating energy. These properties are comparable to the passive elastic properties of muscles within the physiological range of sarcomere length14 and so these materials represent a new muscle-mimetic biomaterial. The mechanical properties of these biomaterials can be fine-tuned by adjusting the composition of the elastomeric proteins, providing the opportunity to develop biomaterials that are mimetic of different types of muscles. We anticipate that these biomaterials will find applications in tissue engineering15 as scaffold and matrix for artificial muscles.