Recently, a procedure was suggested to synthesize polymers with characteristics similar to those observed in globular proteins : renaturability and the existence of an "active site" capable of specifically recognizing a given target molecule. This procedure was originally studied using a computer simulation of the thermodynamics of lattice 27-mers. This analysis is extended to the thermodynamic study of longer chains (36-mers) and different types of short range interactions. We found, in the best conditions, a 50% success rate of creating renaturable heteropolymers, thus confirming the original results. Folding kinetics as examined by Monte Carlo simulation show that the imprinted sequences can reach the ground state reliably and quickly. Finally, we compare the correlations found in the imprinted sequences with those found in natural proteins. We interpret these results as the confirmation of the efficacy of the polymerization procedure.