For the small peptide met-enkephalin in implicit aqueous solvent a connected database of potential energy minima and transition states is constructed and refined based on kinetic criteria, using the discrete path sampling method. A comparison of this technique with parallel tempering Monte Carlo simulations shows that it produces a satisfactory sampling of the configuration space occupied at 298 K. The peptide is predicted to show a folding transition, and time scales for this folding are obtained, along with a description of significant folding intermediates. (C) 2003 American Institute of Physics.