The addition of Graphene Oxide (GO) into the recombinant silk protein secreted from Pichia Pastoris is analyzed to see if they can bond together to form an enhanced material when the protein is regenerated. Raman spectroscopy showed the presence of GO in the protein containing a 10% w/v GO/dope solution, with the conjugated pi-electron system in the lower wavelengths but did not show new functional groups form revealing that no new bonds formed. While the graphene oxide has replaced some of the hydrogen bonds when presented to the protein in its unraveled structure, the hydroxyl groups of graphene oxide did not align with the carbonyl of the protein due to steric hindrance. All tests were done on regenerated silk in the form of a membrane instead of woven silk. The regenerated silk is hydrophilic and with the presence of GO becomes hydrophobic.