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Updated: May 22, 2026

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
Published on: June 23, 2022
Structural studies of amyloids by quenched hydrogen-deuterium exchange by NMR
Marçal Vilar1, Lei Wang, Roland Riek
1Neurodegeneration Unit, Centro Nacional de Microbiología, Instituto de Salud Carlos III, Madrid, Spain. mvilar@isciii.es
Abstract:
The elucidation of the structure of amyloid fibrils 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.
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