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Infectious and Noninfectious Amyloids of the HET‐s(218–289) Prion Have Different NMR Spectra
Author(s) -
Wasmer Christian,
Soragni Alice,
Sabaté Raimon,
Lange Adam,
Riek Roland,
Meier Beat H.
Publication year - 2008
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.200704896
Subject(s) - infectivity , fibril , prion protein , chemistry , nmr spectra database , amyloid (mycology) , biophysics , biology , virology , biochemistry , spectral line , medicine , pathology , virus , disease , physics , astronomy , inorganic chemistry
The molecular basis for prion infectivity is not yet understood. The NMR spectra of noninfectious and infectious amyloids of the prion‐forming domain 218–289 of the fungal prion HET‐s are clearly different (see picture) but are indicative for a cross‐β arrangement in both cases. The fibrils formed at pH 3 are not infectious because their molecular structure apparently differs substantially from that formed at physiological pH.

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