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Updated: Jul 16, 2025

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
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高度会导致脂质界面上垂直的α-synuclein构造

Steven J Roeters1,2, Kris Strunge3, Kasper B Pedersen3

  • 1Department of Chemistry, Aarhus University, Langelandsgade 140, 8000, Aarhus C, Denmark. s.j.roeters@amsterdamumc.nl.

Nature communications
|September 18, 2023
PubMed
概括

脂质膜影响与帕金森病相关的α-synuclein (αS) 聚合. 高度导致αS采用直立形状,促进相互作用和粉样蛋白形成.

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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