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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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Morphology-Dependent Interactions between α-Synuclein Monomers and Fibrils.

Tinna Pálmadóttir1, Christopher A Waudby2,3, Katja Bernfur1

  • 1Biochemistry and Structural Biology, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.

International Journal of Molecular Sciences
|March 29, 2023
PubMed
Summary

Two distinct alpha-synuclein fibril structures, A and B, form under identical conditions, differing in surface properties and stability. Morphology B fibrils are more stable and convert from morphology A over time.

Keywords:
NMR spectroscopyaggregationmonomorphicmorphologypolymorphicself-assemblystability

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