SFPQ is a human tumor suppressor protein that regulates many important functions in the cell nucleus including coordination of long non-coding RNA molecules into paraspeckles. The ability of SFPQ to form linear polymer molecules via its coiled-coil interactions is essential for the function of the protein in gene regulation.

The project aims to study polymerization of SFPQ by creating truncated protein constructs at coiled-coil region and mutating the key residues. SFPQ coiled-coil interactions will be studied by Small-Angle X-Ray scattering. Previous experiments of SFPQ samples with extended coiled-coil showed increased degree of aggregation at higher concentrations, which clouded results and interfered with accurate studies of SFPQ mutants. Other used techniques for protein interaction studies, such as AUC and SEC, seemed to disrupt protein interactions and caused truncations.