RNA Recognition Motifs (RRMs) are the most common type of protein domain found in eukaryotic RNA-binding proteins (RBPs). They regulate gene expression, RNA processing, and other important cellular processes. These functions of RRMs are dependent on their RNA recognition mode. However, the mechanism of binding between the RRM domain(s) of proteins and RNA is still an active area of investigation. Herein, we report the results of studies relating to the effect of aromatic amino acid mutations on the efficacy of RRM-RNA binding. Briefly, the RRM domain of CELF 2 protein and its six mutant complexes (F135Y, F152Y, F155Y, F176Y, F179Y, F209Y) were examined using Molecular Dynamics (MD). The mutations were introduced at aromatic amino acid phenylalanine (Phe) positions on the RRM2 Domain, substituting each Phe with tyrosine (Tyr). The binding interactions between the mutant and wild-type protein complexes were compared and studied. Comprehensive computational analysis was conducted to determine the effect of mutation on the stability of the protein structure and its interaction with RNA by doing RMSD/RMSF, BSA, PCA and MM/PBSA analysis. It was observed that induced mutations result in structure instability and flexibility, but the binding becomes stronger when Tyr replaced Phe in most mutation complexes. The mutation F135Y located on RRM showed a similar trend to the wild type in terms of binding interaction and stability. These results corelate with the finding that aromatic amino acids play a crucial role in RRM-RNA binding. This study offers insight into the RNA-binding mechanism and encourages further studies into the role of RRM primary sequence towards RNA binding.