Structural model of the amyloid fibril formed by beta(2)-microglobulin #21-31 fragment based on vibrational spectroscopy.
A structural model of amyloid fibril formed by the #21-31 fragment of beta2-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 beta-sheet structure. Raman spectra indicated the formation of a dimer with a disulfide bridge between C25 residues.
Hiramatsu
Hirotsugu
H
Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki 444-8787, Japan.
Goto
Yuji
Y
Naiki
Hironobu
H
Kitagawa
Teizo
T
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013055:Spectrophotometry, Infrared; D013059:Spectrum Analysis, Raman; D001613:beta 2-Microglobulin / Q000737:chemistry*
D000682:Amyloid; D010446:Peptide Fragments; D001613:beta 2-Microglobulin