Here we have combined rigorous umbrella sampling and parallel bias metadynamics to understand the specificity of amino acids (D-and L-arginine) to the folding-unfolding equilibria of a 12-mer GAAA RNA hairpin motif. We constructed the free energy landscape using multiple collective variables of RNA folding in presence of either D-or L-arginine. Our results show that the free energy surface of the folded state is stabilized only in presence of D-arginine and destabilized in presence of L-arginine. Interestingly, the misfolded states were of similar free energy with respect to the extended unfolded state.