Using molecular dynamics simulations to calculate free energies of molecular transformation, we have computed helix-coil transition free energies for alanine oligomers up to 14 residues long. The simulations have been done on the model in vacuo with dielectric constant, epsilon = 1, 5, 25, and infinity and on the model in solution with explicit representation of water molecules and with partial charges on the oligomer set to zero. (The analogous simulations of the solvated model with full charges on the oligomer were reported elsewhere [L. Wang et al. (1995) Proceedings of the National Academy of Science USA 92, 10924-10928]). In vacuo, both entropic and electrostatic contributions oppose formation of a 3-residue helical nucleus in the helix initiation step. The entropy change opposing helix growth is found to be 3 e.u., van der Waals interactions favor helix growth by 1.9 kcal/mol, and electrostatic interactions favor helix growth by 3 kcal/mol (for epsilon = 1; all these values are per residue). In water, helix stability is slightly greater for the zero-charge model than for the full-charge model, i.e., the polypeptide's electrostatic interactions, which include hydrogen bonds, slightly destabilize the helix. The helix stabilizing contribution of the hydrophobic effect was found to be identical to that of the van der Waals interactions in vacuo (i.e., 1.9 kcal/mol per residue). The zero-charge model has nearly identical helix stability in vacuo and in water, the almost identical free energies of transfer of helix and coil state of the zero-charge oligomer from vacuum to water are found to be small. Thus, the results of this systematic variation of the force field afford a meaningful decomposition of the free energies for helix initiation and growth.