We explore for a simple artificial peptide, Ala(10)-GIY(5)-Ala(10), the relation between secondary structure formation and folding and its dependence on the solvent model. Our data rely on multicanonical Monte Carlo simulations where the interactions among all atoms are taken into account. Three implicit solvent models are considered to approximate the interaction between protein and the surrounding water, and the results are compared to previous data from gas-phase simulations. Our data indicate that the final structure and the details of the folding process depend strongly on how the solvent environment affects secondary structure formation.