Answer:
A few obstacles would make it tough to accomplish this objective. In the first place, the polypeptide backbone is characteristically polar. Hardly any proteins would be dissolvable in a non-polar hydrocarbon. Moreover, to keep up the dissolvability of this protein, most of its amino acids would need to contain hydrophobic or non-polar R groups.
Then again, its charged or polar R groups would need to connect with one another or be covered in the core of the protein away from the hydrocarbon solvent. This would put noteworthy requirements on both the idea of the R groups and the structure of the protein that could take part in substrate recognition or catalysis. By and large, this is certainly not a reasonable objective.