Orientation of the infrared transition moments for an alpha-helix.
Appropriate values for the orientation of the amide transition dipoles are essential to the growing use of isotopically edited vibrational spectroscopy generally in structural biology and to infrared dichroism measurements on membrane-associated alpha-helices, in particular. The orientations of the transition moments for the amide vibrations of an alpha-helix have been determined from the ratio of intensities of the A- and E(1)-symmetry modes in the infrared spectra of poly(gamma-methyl-L-glutamate)(x)-co-(gamma-n-octadecyl-L-glutamate)( y) oriented on silicon substrates. Samples possessing a high degree of alignment were used to facilitate band fitting. Consistent results were obtained from both attenuated total reflection and transmission experiments with polarized radiation, yielding values of Theta(I) = 38 degrees, Theta(II) = 73 degrees, and Theta(A) = 29 degrees, relative to the helix axis, for the amide I, amide II, and amide A bands, respectively. The measurements are discussed both in the context of the somewhat divergent older determinations, and in relation to the helix geometry and results on model amide compounds, to resolve current uncertainties in the literature.
Marsh
D
D
Max-Planck-Institut für biophysikalische Chemie, Abteilung Spektroskopie, D-37070 Göttingen, and Institut für Polymerforschung, D-01005 Dresden, Germany. dmarsh@gwdg.de
Müller
M
M
Schmitt
F J
FJ
D055592:Biophysical Phenomena; D001703:Biophysics; D066298:In Vitro Techniques; D008956:Models, Chemical; D010455:Peptides / Q000737:chemistry*; D011099:Polyglutamic Acid / Q000031:analogs & derivatives / Q000737:chemistry; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
D010455:Peptides; C030315:poly-gamma-methylglutamate; D011099:Polyglutamic Acid