Natural proteins perform a variety of functions in biological systems, including actuation, catalysis, structural support, and molecular sequestering. The variety of natural protein functions suggest that they could serve as valuable and versatile building blocks for synthesis of functional materials. Based on this premise, several investigators have developed schemes to include functional proteins into hydrogel networks to take advantage of their structural, catalytic, and ligand binding properties. Natural proteins such as collagen [1] and elastin [2] have been used to develop materials with tailored structural and mechanical properties, while catalysis by enzymes (e.g., glucose oxidase [3] ) has been used to build smart, environmentally-responsive hydrogel networks. The ability of proteins to selectively bind ligands has been used to develop materials that change their degree of physical or chemical crosslinking in the presence of biological antigens, [4,5] small molecule drugs, [6] and carbohydrates, [7][8][9] resulting in environmentallyresponsive biomaterials. In each of these previous studies a nanometer-scale function associated with a specific protein was exploited to build a material that performed an intriguing macroscopic function. A function that has not been explored as extensively in materials science is the ability of proteins to undergo complex conformational changes. Proteins change conformations in response to a broad range of stimuli, including light, pH, and the binding of biological molecules. Over 200 conformational changes are well-characterized, [10] representing a vast unexplored databank of molecular building blocks for design of dynamic materials. Recent studies have demonstrated the utility of protein conformational changes in nano-scale engineered systems, including cooperative nanometer-scale motors [11] and molecular shuttles, [12] suggesting that dynamic protein molecules could also be a useful component of 3-dimensional materials. To that end, we recently reported an approach that used a dynamic protein as a partial cross-linker in a chemically cross-linked hydrogel network, and these hydrogels changed their volume in the presence of a specific protein-binding molecule.[13] Here we describe assembly of protein-based, dynamic materials using a novel photochemical approach. This approach allows for high concentrations of protein to be functionally included into a network in response to light, and the resulting materials undergo striking volume changes upon protein-ligand binding. Photochemical assembly also enables spatial control over the location of dynamic proteins in a hydrogel network, which is likely to be important in potential materials science and engineering applications.