Related Experiment Video
Updated: May 8, 2026

07:56
Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
Published on: May 30, 2021
Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy
S Pornsuwan1, K Giller, D Riedel
1Research Group EPR Spectroscopy, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany) http://www.mpibpc.mpg.de/english/research/ags/bennati/; Current address: Department of Chemistry, Faculty of Science, Mahidol University, 10400 Bangkok (Thailand).
Angewandte Chemie (International Ed. in English)
|August 13, 2013
Abstract
No abstract available in PubMed .
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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, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
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, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...

