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

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 44, 2005, Pages 15871-15876

  Heise, Henrike ^a   Hoyer, Wolfgang ^a   Becker, Stefan ^a   Andronesi, Ovidiu C ^a   Riedel, Dietmar ^a   Baldus, Marc ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

Amyloid; EM; Parkinson's disease; Protein aggregation; Protein structure

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; CARBON 13; NITROGEN 15;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DNA POLYMORPHISM; IMAGE ANALYSIS; ISOTOPE LABELING; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SEQUENCE ANALYSIS; SOLID STATE; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING;

ALPHA-SYNUCLEIN; CARBON ISOTOPES; CLONING, MOLECULAR; HUMANS; KINETICS; MOTION; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

EID: 27644518721     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0506109102     Document Type: Article

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