%0 Journal Article
%A Heise, H.
%A Celej, M.S.
%A Becker, S.
%A Riedel, D.
%A Pelah, A.
%A Kumar, A.
%A Jovin, T.M.
%A Baldus, M.
%T Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein
%J Journal of molecular biology
%V 380
%@ 0022-2836
%C Amsterdam [u.a.]
%I Elsevier
%M PreJuSER-276
%P 444 - 450
%D 2008
%Z Record converted from VDB: 12.11.2012
%X Fibrils from the Parkinson's-disease-related A53T mutant of alpha-synuclein were investigated by solid-state NMR spectroscopy, electron microscopy, and atomic force microscopy. Sequential solid-state NMR resonance assignments were obtained for a large fraction of the fibril core. Experiments conducted above and below the freezing point suggest that the fibrils contain regions with increased mobility and structural elements different from beta-strand character, in addition to the rigid beta-sheet-rich core region. As in earlier studies on wild-type alpha-synuclein, the C-terminus was found to be flexible and unfolded, whereas the main core region was highly rigid and rich in beta-sheets. Compared to fibrils from wild-type alpha-synuclein, the well-ordered beta-sheet region extends to at least L38 and L100. These results demonstrate that a disease-related mutant of alpha-synuclein differs in both aggregation kinetics and fibril structure.
%K Amino Acid Sequence
%K Escherichia coli: genetics
%K Freezing
%K Humans
%K Microscopy, Atomic Force
%K Microscopy, Electron
%K Molecular Sequence Data
%K Mutation
%K Nuclear Magnetic Resonance, Biomolecular: methods
%K Parkinson Disease: genetics
%K Parkinson Disease: pathology
%K Protein Structure, Secondary
%K Recombinant Proteins: chemistry
%K Recombinant Proteins: metabolism
%K Recombinant Proteins: ultrastructure
%K alpha-Synuclein: chemistry
%K alpha-Synuclein: genetics
%K alpha-Synuclein: metabolism
%K alpha-Synuclein: ultrastructure
%K Recombinant Proteins (NLM Chemicals)
%K alpha-Synuclein (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:18539297
%U <Go to ISI:>//WOS:000257564000002
%R 10.1016/j.jmb.2008.05.026
%U https://juser.fz-juelich.de/record/276