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• W2324573711 abstract "A combined approach, using Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) and solid-state NMR (Nuclear Magnetic Resonance), shows a high degree of polymorphism exhibited by Aβ species in forming hydrogen-bonded networks. Two Alzheimer’s Aβ peptides, Ac-Aβ16–22-NH2 and Aβ11–25, selectively labeled with 17O and 15N at specific amino acid residues were investigated. The total amount of peptides labeled with 17O as measured by FTICR-MS enabled the interpretation of dephasing observed in 15N{17O}REAPDOR solid-state NMR experiments. Specifically, about one-third of the Aβ peptides were found to be involved in the formation of a specific >C═17O···H–15N hydrogen bond with their neighbor peptide molecules, and we hypothesize that the rest of the molecules undergo ± n off-registry shifts in their hydrogen bonding networks." @default.
• W2324573711 created "2016-06-24" @default.
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• W2324573711 date "2016-04-01" @default.
• W2324573711 modified "2023-10-13" @default.
• W2324573711 title "Amyloid Hydrogen Bonding Polymorphism Evaluated by ¹⁵N{¹⁷O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry" @default.
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• W2324573711 doi "https://doi.org/10.1021/acs.biochem.5b01095" @default.
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