The present study aims to gain a molecular understanding of the preference of a particular chirality in amino acids on RNA tetraloop folding. For that, we constructed here multi-dimensional free energy landscapes of folding-unfolding equilibria of GAAA tetraloop (with sequence 5'-gggcGAAAgccc-3') in presence of D-and L-arginine. The choice of arginine amongst other amino acids is due to its diverse binding capabilities with RNA. Due to the presence of double-sided polar groups and long hydrophobic tail, arginine can bind RNA in the groove as well as stack with the base pairs with specific binding affinities. It is to be noted that the binding affinity and stereospecificity of amino acids towards RNA motifs is highly dependent on the choice of interest of RNA motifs.