Dataset supporting: 'Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High Resolution FTICR-MS (original) (raw)

2016

Abstract

A complementary study, using FTICR-MS and solid-state NMR, shows a high degree of polymorphism exhibited by Aβ species in forming hydrogen-bonded networks. Two Alzheimer’s Aβ peptides selectively labeled with 17O and 15N were investigated. Using 15N{17O}REAPDOR solid-state NMR, the peptides involved in forming hydrogen bond were determined, while the total amount of peptides labeled with 17O was measured by FTICR-MS. About one-third of the Aβ peptides were found involved in the formation of the specific >C=17O···H–15N hydrogen bond with their neighbor peptide molecules, and the rest of the molecules likely undergo ± n off-registry shifts.

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