In silico data were in qualitative agreement with experiments in solution. Detailed analyses were performed on the trajectories extracted from MD simulations of a single homo-or hetero-chiral peptide in explicit water. For each peptide, we performed a MD simulation of 1 µs in length at 298 K, followed by heating to 363 K in 20 ns, and finally an equilibrium simulation of 1 µs at this temperature. We analyzed the secondary structural content and the Ramachandran plot (reported only for the 2nd and 3rd residues of the tetrapeptide, that is those for which both angles can be calculated), the preferred conformations, the end-to-end intramolecular distances, the frequency of formation of intramolecular H-bonds, and the peptide hydration. The heterochiral peptide displayed an intrinsic propensity towards turns (Table ). Importantly, this feature seemed to be energy-driven and temperature-independent (i.e., there was no entropic gain with heating). The opposite was true for the homochiral analog, whose structural preference towards turns at rt was halved as compared to the heterochiral isomer (Table ). The Cα1-to-Cα4 distance (Fig. ) was significantly longer for the homochiral peptide (visiting extended conformations) relative to the heterochiral one (adopting turns). MD confirmed the formation of an intramolecular salt bridge between termini, and the engagement of Phe4 NH in intramolecular H-bonding, and of Phe3 and Leu NH to a lesser extent, in agreement with NMR data (Table ).