Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core

Science

Volumn 319, Issue 5869, 2008, Pages 1523-1526

  Wasmer, Christian ^a   Lange, Adam ^a   Van Melckebeke, Hélène ^a   Siemer, Ansgar B ^a,b   Riek, Roland ^a   Meier, Beat H ^a  

^a ETH ZURICH   (Switzerland)

^b Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; ASPARAGINE; PRION PROTEIN; PROTEIN HET S[218-289]; UNCLASSIFIED DRUG;

AMINO ACID; EXPERIMENTAL STUDY; MODEL; NUCLEAR MAGNETIC RESONANCE; PROTEIN;

ARTICLE; BETA SHEET; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PODOSPORA ANSERINA; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; SOLID STATE;

AMINO ACID SEQUENCE; AMYLOID; FUNGAL PROTEINS; HYDROGEN BONDING; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PODOSPORA; PRIONS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

FUNGI; PODOSPORA ANSERINA; SOLENOIDEA;

EID: 40849120669     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1151839     Document Type: Article

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40. We thank C. Ritter for support in producing the samples, S. Saupe for scientific discussions, and the Swiss National Science Foundation and the TH-system of the ETH Zurich for financial support. H.V.M. acknowledges a stipend by the European Union (Marie Curie EIF, FP6) and A.L. by the European Molecular Biology Organization (EMBO). The bundle of 20 conformers representing the NMR structure has been deposited in the Protein Data Bank with accession code 2RNM, and assignments have been deposited in the Biological Magnetic Resonance Data Bank (ID 11028).