Observation of highly flexible residues in amyloid fibrils of the HET-s prion.

@article{Siemer2006ObservationOH,
  title={Observation of highly flexible residues in amyloid fibrils of the HET-s prion.},
  author={Ansgar B Siemer and Alexandre Arnold and Christiane Ritter and Thomas Westfeld and Matthias Ernst and Roland Riek and Beat H Meier},
  journal={Journal of the American Chemical Society},
  year={2006},
  volume={128 40},
  pages={13224-8}
}
We report the observation of undetected (until now) residues of the prion protein fragment HET-s(218-289) which give rise to well-resolved (13)C, (15)N, and (1)H NMR resonances under high-resolution magic-angle spinning (HRMAS) conditions. The observed signals belong to large polymeric units as shown by measuring the lateral diffusion constants. The amino acids identified in the spectra are compatible with their localization in the segments of the protein which could not be detected in earlier… CONTINUE READING

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