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It had been previously discovered in our lab that the native dragline silk of golden orbweaver (Nephila clavipes) contains two proteins with distinct sequence features: major ampullate spidroin 1 (MaSp1) and major ampullate spidroin 2 (MaSp2). Each protein has some unique motifs that we believe to control the tensile strength and elasticity etc. They are the main factor responsible for the extraordinary mechanical property of spider silk. Early works in this field have expressed both synthetic MaSp1 and MaSp2 proteins individually from various type of host organisms, and spun into fibers in vitro. My current work focus on creating a spider silk protein that contains the sequence features of both MaSp1 and MaSp2, express this chimeric protein in E. coli. and spun it into fibers for mechanical property test. With a full set of motifs from both MaSp1 and MaSp2 and a more evenly distributed protein structure, I hope to see some mechanical property improvements as compared with synthetic fibers containing solely MaSp1 or MaSp2, or fiber pulled from MaSp1 and MaSp2 mixture.