Fourier transform infrared spectra of the polypeptide alamethicin and a possible structural similarity with bacteriorhodopsin.

FTIR spectra of alamethicin have been obtained in KBr disk, methanol and in aqueous lipid dispersion (above and below the lipid phase transition). The solution structure of this polypeptide in methanol has been shown by recent studies (Esposito et al. (1987) Biochemistry 26, 1043-1050) using NMR spectroscopy to be predominantly alpha-helical in content. It may therefore be regarded as a model structure for the interpretation of the spectra of certain biomembrane proteins. A comparison of the spectra with that obtained with bacteriorhodopsin shows spectral similarities, e.g. the presence of a high-frequency amide I maximum at 1661-1663 cm-1 and shoulders near 1640 cm-1 and 1620 cm-1.