In this article, we report on a computational investigation of the binding of activated ribonucleotides in nonenzymatic RNA template copying. In particular, we employ molecular dynamics (MD) simulations based on classical force fields to investigate the binding of different imidazole-bridged dinucleotide intermediates to the templating strand, just below the 3 ′ -end of the copied strand. These results demonstrate that the rate and fidelity of nonenzymatic template copying is governed by more subtle structural and dynamical effects than simply the number of hydrogen bonds in the Watson-Crick base pairing pattern, or the thermodynamic stability of a given base pair.