Development of new drugs is always necessary for the betterment of human healthcare. Whether it be new antibiotics or medicines for viral disease. One strategy is to target certain proteins. To be able to develop these kinds of medicines, the protein itself must be understood. This can be done by biochemical and biophysical characterization of the studied protein. In this thesis, the biophysical characterization of one such protein, ZC3H11A, will be explored. Here, the aim is to understand how the protein behaves and how structurally it looks like. This is achieved by first attaining the protein in a highly pure and stable form. Then doing interaction studies with surface plasmon resonance-based biosensors, measuring the size by dynamic light scattering, and with structural studies in the form of circular dichroism, crystallization, and cryo electron microscopy. The results show that this intrinsically disordered protein binds very strongly to RNA containing loop secondary structures. It was also shown that the protein was prone to aggregation at lower pH than pH 9. Further, the structural studies show that one single representative model is difficult to obtain, likely due to the disordered nature. None the less, a structure was obtained which can be used to guide further optimization of sample preparation and data collection. In the end, it was shown that ZC3H11A is sensitive to both salt concentrations and pH. It was also shown how to rid the sample of nucleic acids. These results will help in future studies of how this disordered protein works.