Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of ?-synuclein.
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ABSTRACT:
SUBMITTER: Haney CM
PROVIDER: S-EPMC5961496 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
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Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of α-synuclein.
Haney Conor M CM Petersson E James EJ
Chemical communications (Cambridge, England) 20180101 7
The neuronal protein α-synuclein (αS) plays a key role in Parkinson's disease, forming inclusions termed Lewy bodies and Lewy neurites. Recent improvements in cryo-electron diffraction and solid state NMR (ssNMR) have led to the elucidation of the structures of peptides derived from the αS fibril core and full-length human αS in fibrils. Despite the valuable insight offered by these methods, there are still several questions about the structures' relevance to pathological aggregates. Herein, we ...[more]
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