Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15871-6 doi: 10.1073/pnas.0506109102. 2005 Oct 24.

Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR

Heise H, Hoyer W, Becker S, Andronesi OC, Riedel D, Baldus M.


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 AS reverse-labeled for two of the most abundant amino acids, K and V, were analyzed. (13)C and (15)N signals exhibited linewidths of

PMID: 16247008