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High‐Resolution Solid‐State NMR Spectroscopy of the Prion Protein HET‐s in Its Amyloid Conformation
Author(s) -
Siemer Ansgar B.,
Ritter Christiane,
Ernst Matthias,
Riek Roland,
Meier Beat H.
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200462952
Subject(s) - prion protein , nuclear magnetic resonance spectroscopy , amyloid (mycology) , chemistry , crystallography , high resolution , solid state nuclear magnetic resonance , spectroscopy , resolution (logic) , protein structure , nuclear magnetic resonance , stereochemistry , physics , biochemistry , medicine , inorganic chemistry , remote sensing , disease , pathology , quantum mechanics , artificial intelligence , computer science , geology
Partly present, partly absent: The solid‐state NMR spectra (figure, right side) of the amyloid form of the HET‐s prion protein (EM image at left) show the resonances for 43 residues with high resolution, whereas 29 residues give no observable NMR signals. A possible explanation could be that the protein structure consists of both highly ordered and strongly disordered domains.