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Updated: Jun 27, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance
Anders Olofsson1, A Elisabeth Sauer-Eriksson, Anders Ohman
1Umeå Center for Molecular Pathogenesis, Umeå University, Umeå, Sweden. anders.olofsson@ucmp.umu.se
Abstract:
A general method to explore the dynamic nature of amyloid fibrils is described, combining hydrogen/deuterium exchange and nuclear magnetic resonance spectroscopy to determine the exchange rates of individual amide protons within an amyloid fibril. Our method was applied to fibrils formed by the amyloid-beta(1-40) peptide, the major protein component of amyloid plaques in Alzheimer's disease. The fastest exchange rates were detected among the first 14 residues of the peptide, a stretch known to be poorly structured within the fibril. Considerably slower exchange rates were observed in the remainder of the peptide within the beta-strand-turn-beta-strand motif that constitutes the fibrillar core.
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