Arginine methylation is a post-translational protein modification that is catalyzed by proteins known as arginine methyl transferases (RMTs). Recently, arginine methylation was postulated as an important modification in modulating biomolecular interactions. RMTs largely target nuclear proteins, so it is highly likely that they aid in modulating protein...DNA interactions. In this study, we probe the influence that sequential guanidinium methylation has on the energetics of the guanidinium...guanine and guanidinium...guanine...cytosine complexes using ab initio and double-hybrid density functional theory (DFT) methods. Structures of guanidiniurn...guanine complexes derived at the MP2/6-31+G** level of theory show that monomethylated, symmetrically dimethylated, and unsymmetrical dimethylated guanidiniums, are all capable of forming guanidinium...guanine complexes. However, when cytosine is involved in a base pair to guanine, only the monomethylated and symmetrically dimethylated guanidinium groups are capable of forming hydrogen bond complexes with guanine. At the B2-PLYP/6-311++G** level of theory, we found that methylation of the guanidinium group stabilizes the formation of the guanidinium...guanine complex relative to the unmethylated guanidinium...guanine complex by similar to 2.5 kcal mol(-1). The biological implication of these findings are discussed.