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Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
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Direct evidence of coexisting horseshoe and extended helix conformations of membrane-bound alpha-synuclein

Marta Robotta1, Patrick Braun, Bart van Rooijen

  • 1Department of Chemistry, University of Konstanz, Universitätsstr. 10, 78457 Konstanz, Germany.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry
|January 29, 2011
PubMed
Abstract

No abstract available in PubMed .

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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. 
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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, normally used to...

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