  A method to reconstruct the energy landscape of small peptides is presented
with reference to a 2d off--lattice model. The starting point is a statistical
analysis of the configurational distances between generic minima and directly
connected pairs (DCP). As the mutual distance of DCP is typically much smaller
than that of generic pairs, a metric criterion can be established to identify
the great majority of DCP. Advantages and limits of this approach are
thoroughly analyzed for three different heteropolymeric chains. A funnel--like
structure of the energy landscape is found in all of the three cases, but the
escape rates clearly reveal that the native configuration is more easily
accessible (and is significantly more stable) for the sequence that is expected
to behave as a real protein.
