We describe the biosynthesis and characterization of protein materials
comprised of two distinct self-assembling domains (SADs): elastin (E) found
in tissue for its elastic properties and cartilage oligomeric matrix protein
coiled-coil (COMPcc, C) predominantly locatedin joint and in bones. Based on
earlier studies on protein block polymers comprised these two SADs,
orientation and number of blocks play a crucial role in the overall
stimuli-responsive supramolecular assembly behavior. Here we fabricate a
range of EnC and CEn block polymers in which the E
domain is systematically truncated to explore the effects of the E domain on
the overall physicochemical behavior.