We study the relation between alpha-helix formation and folding for a simple artificial peptide, Ala(10)-Gly(5)-Ala(10). Our data rely on multicanonical Monte Carlo simulations where the interactions among all atoms are taken into account. The free-energy landscape of the peptide is evaluated for various temperatures. Our data indicate that folding of this peptide is a two-step process. In the first step two alpha-helices are formed which afterwards re-arrange themselves into a U-like structure.