Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy
نویسندگان
چکیده
منابع مشابه
Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.
The 140-residue protein alpha-synuclein (AS) is able to form amyloid fibrils and as such is the main component of protein inclusions involved in Parkinson's disease. We have investigated the structure and dynamics of full-length AS fibrils by high-resolution solid-state NMR spectroscopy. Homonuclear and heteronuclear 2D and 3D spectra of fibrils grown from uniformly (13)C/(15)N-labeled AS and A...
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ژورنال
عنوان ژورنال: eLife
سال: 2019
ISSN: 2050-084X
DOI: 10.7554/elife.48907