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Solid‐State NMR Spectroscopy Reveals that <i>E. coli</i> Inclusion Bodies of HET‐s(218<b>–</b>289) are Amyloids
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Citations
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References
2009
Year
Protein SecretionMolecular BiologyProtein DepositionProtein ExpressionProtein FoldingPrion DiseaseProtein MisfoldingProteomicsBiophysicsBiochemistryInclusion BodiesSolution Nmr SpectroscopyPrion InfectivityStructural BiologyNatural SciencesPathogenesisProtein NmrMicrobiologyMedicineNuclear Magnetic Resonance Spectroscopy
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.
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