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Updated: May 29, 2026
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids
Christian Wasmer1, Laura Benkemoun, Raimon Sabaté
1Laboratorium für Physikalische Chemie, ETH Zurich, 8093 Zurich, Switzerland.
Angewandte Chemie (International Ed. in English)
|May 28, 2009
Abstract:
Protein deposition frequently occurs as inclusion bodies (IBs) during heterologous protein expression in E. coli. The structure of these E. coli IBs of the prion-forming domain from the fungal prion HET-s is the same as that previously determined for fibrils assembled in vitro, and show prion infectivity. These results demonstrate that the IBs of HET-s(218-289) are amyloids.
