Raman optical activity (ROA) reveals surprising details of the secondary structure of polypeptides and proteins in solution phase. Yet specific spectral features, such as in the extended amide III region of hydrated α-helix, did not seem explicable by the generally accepted sensitivity of ROA to the local conformation. This is reconciled in the present study by simulations of ROA spectra for model α-helical structures. Two positive ROA peaks often observed at around 1340 and 1300 cm(-1) for polypeptides and proteins have been assigned to two types of solvated α-helices; one is stable in hydrophilic environment where amide groups make hydrogen bonds to solvent molecules or polar side chains (∼1340 cm(-1)), and the other is supported by a hydrophobic environment without the possibility of external hydrogen bonds (∼1300 cm(-1)). For poly-L-alanine (PLA), regarded as a good model of α-helical structure, the experimentally observed relative intensity ratio of the two ROA bands has been explained by a conformational equilibrium depending on the solvent polarity. The intensities of the bands reflect solvated and unsolvated α-helical geometries, with peptide backbone torsional angles (ϕi+1, ψi) of (-66°, -41°) and (-59°, -44°), respectively. Quantum-mechanical simulations of the ROA spectra utilizing the normal mode optimization and Cartesian tensor transfer methods indicate, however, that the change in dielectric constant of the solvent is the main factor for the spectral intensity change, whereas the influence of the conformational change is minor.