ArticleThe journal of physical chemistry. B2012
Dissecting two-dimensional ultraviolet spectra of amyloid fibrils into beta-strand and turn contributions.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
We present an analysis of the contributions of various secondary structure elements of the amyloid β-protein to the two-dimensional far ultraviolet (2DFUV) signal of an amyloid fibril model. The contributions of the turns and the β-strands are affected by the geometry of the backbone peptide amide π → π* transition dipoles, the backbone interamide coupling in the excited state, and the exciton delocalization. These contributions are clearly distinguishable in the xyxy-xyyx pulse polarization configuration. The differences are attributed to the smaller splitting of the exciton energies and the larger fluctuations of the geometry of the peptide amide π → π* transition dipoles at the turns, while making the 2DFUV signal sensitive to the secondary structure. This signal may be used to determine the proportion of turns and β-strands.
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