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Kim, Yung Sam
Ultrafast 2D IR Spectroscopy Lab
Research Interests
  • 2D IR, chemical exchange of H-bond, fast reaction dynamics, protein dynamics

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Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from A beta 40

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Title
Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from A beta 40
Author
Kim, Yung SamLiu, LiuAxelsen, Paul H.Hochstrasser, Robin M.
Keywords
β-amyloid 40; Exciton; Two-dimensional infrared spectroscopy
Issue Date
2008-06
Publisher
NATL ACAD SCIENCES
Citation
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OFAMERICA, v.105, no.22, pp.7720 - 7725
Abstract
The 2D IR spectra of the amide-I vibrations of amyloid fibrils from Aβ40 were obtained. The matured fibrils formed from strands having isotopic substitution by 13C=18O at Gly-38, Gly-33, Gly-29, or Ala-21 show vibrational exciton spectra having reduced dimensionality. Indeed, linear chain excitons of amide units are seen, for which the interamide vibrational coupling is measured in fibrils grown from 50% and 5% mixtures of labeled and unlabeled strands. The data prove that the 1D excitons are formed from parallel in-register sheets. The coupling constants show that for each of the indicated residues the amide carbonyls in the chains are separated by 0.5 ± 0.05 nm. The isotope replacement of Gly-25 does not reveal linear excitons, consistent with the region of the strand having a different structure distribution. The vibrational frequencies of the amide-I modes, freed from effects of amide vibrational excitation exchange by 5% dilution experiments, point to there being a component of an electric field along the fibril axis that increases through the sequence Gly-38, Gly-33, Gly-29. The field is dominated by side chains of neighboring residues.
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DOI
10.1073/pnas.0802993105
ISSN
0027-8424
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PHY_Journal Papers
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