After our explorations of self-assembling homopolymers, we are now investigating translational fusion proteins that combine the poly(EAK)n domain with another structural or functional element. Preliminary experiments indicate that the mechanical and morphological properties of these gels can be tuned by varying characteristics of the amino acid sequence or by changing the identity of the fusion domain. We have also demonstrated the ability to modulate nanoscale feature dimensions and morphology of the hydrogel matrix. In this paper, we describe the challenges of producing these unique biomolecules. We also discuss the physical properties of these structural proteins and the usefulness of fusion proteins incorporating both structural and chemically functional moieties.