We investigate the thermal stability of helical hydrophobic oligomers using a three-dimensional, water-explicit lattice model and the Wang-Landau Monte Carlo method. The degree of oligomer helicity is controlled by the parameter epsilon(mm) < 0, which mimics monomer-monomer hydrogen bond interactions leading to the formation of helical turns in atomistic proteins. We vary vertical bar epsilon(mm)vertical bar between 0 and 4.5 kcal/mol and therefore investigate systems ranging from flexible homopolymers (i.e., those with no secondary structure) to helical oligomers that are stable over a broad range of temperatures. We find that systems with l vertical bar epsilon(mm)vertical bar <= 2.0 kcal/mol exhibit a broad thermal unfolding transition at high temperature, leading to an ensemble of random coils. In contrast, the structure of conformations involved in a second, low-temperature, transition is strongly dependent on le,). Weakly helical oligomers are observed when le,,1 <= 1.0 kcal/mol and exhibit a low-temperature, cold-unfolding-like transition to an ensemble of strongly water-penetrated globular conformations. For higher vertical bar epsilon(mm)vertical bar (1.7 kcal/mol < vertical bar epsilon(mm)vertical bar <= 2.0 kcal/mol), cold unfolding is suppressed, and the low temperature conformational transition becomes a "crystallization", in which a "molten" helix is transformed into a defect free helix. The molten helix preserves >= 50% of the helical contacts observed in the "crystal" at a lower temperature. When vertical bar epsilon(mm)vertical bar = 4.5 kcal/mol, we find that conformational transitions are largely suppressed within the range of temperatures investigated.