Even though extensive effort has been put to parameterize the force fields for RNA and proteins, the RNA-protein complex simulations remain problematic because they need to provide reasonable interactions at the interface of these two chemically different molecules. This study further confirms that the force field and other simulation parameters selection is always dependent on the studied system. Based on our results all the tested non-polarizable force fields can be used to simulate RNAprotein complexes. However, all the non-polarizable force fields tended to make the complexes very compact which might prevent the formation of some biologically relevant conformations. To avoid this, and when the computational cost is not an issue, the polarizable force field AMOEBA could be preferred, but the polarizable O3P water model cannot be recommended for RNA-protein complex simulations. We perceive that the polarizable force fields are the future of biomolecular simulations also beyond the RNA-protein complexes after sufficient development of software and hardware makes them a computationally reasonable alternative.