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Vibrational spectroscopy with inelastic neutron scattering can provide spectra that are more detailed and easier to interpret than optical spectra. The spectral intensity depends on energy transfer and kinetic momentum transfer, allowing determination of the potential function. Experiments reveal that the proton involved in intermolecular hydrogen bonding in N-methylacetamide and polyglycine I vibrates almost independently. An ionic representation (N(delta-)...H(+)...O(delta-)) of the hydrogen bond is more realistic than the normally accepted covalent model (NH...O). For polyglycine I, the proton experiences a local, symmetric double-minimum potential arising from dynamic exchange between the amide-like (CONH) and imidol-like (HOCN) forms of the peptide unit.

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