Studies of peptides forming 3(10)- and alpha-helices and beta-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy.

In order to examine the potential correlation between infrared absorption spectra and 3 10 - and α-helices and β-bend ribbon structures, the secondary structures of synthetic peptides known to contain pure 3 10 -helices, mixed 3 10 /α-helices, and pure β-bend ribbon structures, based upon X-ray diffraction and NMR studies, have been investigated by using FTIR spectroscopy incorporating resolution-enhancement techniques