Infrared spectroscopy is a useful technique for the determination of c
onformation and orientation of membrane-associated proteins and lipids
. The technique is especially powerful for detecting conformational ch
anges by recording spectral differences before and after perturbations
in physiological solution. Polarized infrared measurements on oriente
d membrane samples have revealed valuable information on the orientati
on of chemical groupings and substructures within membrane molecules w
hich is difficult to obtain by other methods. The application of infra
red spectroscopy to the static and dynamic structure of proteins and p
eptides in lipid bilayers is reviewed with some emphasis on the import
ance of sample preparation. Limitations of the technique with regard t
o the absolute determination of secondary structure and orientation an
d new strategies for structural assignments are also discussed.