Ontology highlight
ABSTRACT:
SUBMITTER: Flynn JD
PROVIDER: S-EPMC7269816 | biostudies-literature | 2020 Jun
REPOSITORIES: biostudies-literature
Flynn Jessica D JD Gimmen Megan Y MY Dean Dexter N DN Lacy Shannon M SM Lee Jennifer C JC
Chembiochem : a European journal of chemical biology 20200227 11
Conformational changes in α-synuclein (α-syn) are central to its biological function and Parkinson's disease pathology. Here, terminal alkynes (homopropargylglycine) were employed as environmentally sensitive Raman probes at residues 1, 5, 116, and 127 to characterize soluble (disordered), micelle-bound (α-helical), and fibrillar (β-sheet) α-syn. Along with the full-length protein, a disease-related C-terminal truncation (1-115) was also studied. For the first time, β-sheet α-syn amyloid structu ...[more]