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Updated: Jun 29, 2025

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
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Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

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用小角度散射进行α-synuclein-membrane相互作用和由此产生的聚合的结构性表征

Céline Galvagnion1, Abigail Barclay2, Katarzyna Makasewicz3

  • 1Department of Drug Design and Pharmacology, University of Copenhagen, 2100 Copenhagen, Denmark. celine.galvagnion@sund.ku.dk.

Physical chemistry chemical physics : PCCP
|March 25, 2024
PubMed
概括

脂质通过与像α-synuclein这样的蛋白质相互作用来加速粉样蛋白纤维的形成. 这项研究揭示了脂质积极重组,形成颗粒,后来组装成粉样纤维.

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

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相关概念视频

Amyloid Fibrils03:03

Amyloid Fibrils

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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