Structural Studies of Amyloids by Quenched Hydrogen–Deuterium Exchange by NMR
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Date
2012Type
- Book Chapter
ETH Bibliography
yes
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Abstract
The elucidation of the structure of amyloid fi brils and related aggregates is an important step towards understanding the pathogenesis of diseases such as Alzheimer’s and Parkinson’s, which feature protein misfolding and/or aggregation. However, the large size and poor solubility of amyloid-like fibrils make them resistant to high-resolution structure determination. Here, we describe the use of hydrogen–deuterium exchange coupled with NMR as an indirect strategy to determine the folding regions of amyloid-forming proteins at residue level resolution. Show more
Publication status
publishedBook title
Amyloid ProteinsJournal / series
Methods in Molecular BiologyVolume
Pages / Article No.
Publisher
Humana PressSubject
Amyloid fibrils; H/D exchange; NMR; Aβ, α-synucleinOrganisational unit
03782 - Riek, Roland / Riek, Roland
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ETH Bibliography
yes
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