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TitleAtomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 132, Page 13765-13775, Year 2010
Publish dateMay 20, 2009 (structure data deposition date)
AuthorsVan Melckebeke, H. / Wasmer, C. / Lange, A. / AB, E. / Loquet, A. / Bockmann, A. / Meier, B.H.
External linksJ. Am. Chem. Soc. / PubMed:20828131
MethodsNMR (solid-state)
Structure data

PDB-2kj3:
High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR
Method: SOLID-STATE NMR

Source
  • podospora anserina (fungus)
KeywordsPROTEIN FIBRIL / HET-s(218-289) / BETA-SOLENOID / PRION / AMYLOID FIBRIL / PARALLEL BETA-SHEETS / HYDROPHOBIC CORE / SALT BRIDGES / ASPARAGINE LADDERS / BETA-HELIX

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