2007 Volume 80 Issue 6 Pages 1148-1156
Raman spectra of undeuterated and deuterated rachis from a fowl feather was observed with 488 nm excitation in the 400–1800 cm−1 region. Fowl feather rachis and barbs were subjected to a polarized Raman microscopic examination with excitation at 785 nm. From the observed frequencies, intensities, and scattering anisotropies of the 20 Raman bands, and on the basis of known Raman tensors of the 10 localized molecular vibrations, conformations, and orientations of the polypeptide main chains, tyrosine, phenylalanine, tryptophan residues, and disulfide linkages of the protein molecules in the feather were elucidated.
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