A structural model of amyloid fibril formed by the #21-31 fragment of
2-microglobulin is proposed from microscope IR measurements on specifically
13C-labeled peptide fibrils and Raman spectra of the dispersed fibril solution. The
13C-shifted amide frequency indicated the secondary structure of the labeled residues. The IR spectra have demonstrated that the region between F22 and V27 forms the core part with the extended
-sheet structure. Raman spectra indicated the formation of a dimer with a disulfide bridge between C25 residues.