Search Results - "amyloid"

The structure of amyloid fibrils of the HET-s (218-289) prion as seen by solid-state NMR

Table of Contents: “…Contents: 3D structure is important -- Prion hypothesis -- Prions can form amyloids -- Amyloids -- Cross-beta arrangements give characteristic fiber diffraction patterns -- Solid-state NMR can characterize amyloid fibrils -- Atomic-resolution structure determination by NMR and x-ray -- Distance information in NMR correlation spectra -- The methodology to obtain 3D structures from solid (microcrystalline) samples has recently been developed -- Structure determination is possible -- Nevertheless, amyloids are different -- Isotopic labeling allows to disentangle the intra/inter problem -- HET-s: a functional prion -- Structural information about HET-s (218-289) from earlier measurements -- Chemical shift assignment -- To go further we need distance restraints -- Distance restraints for protein fibrils -- Intramolecular restraints -- Structure calculation -- Structural features of the fibrils -- Comparison with globular proteins.…”
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The structure of amyloid fibrils of the HET-s (218-289) prion as seen by solid-state NMR

Table of Contents: “…Contents: 3D structure is important -- Prion hypothesis -- Prions can form amyloids -- Amyloids -- Cross-beta arrangements give characteristic fiber diffraction patterns -- Solid-state NMR can characterize amyloid fibrils -- Atomic-resolution structure determination by NMR and x-ray -- Distance information in NMR correlation spectra -- The methodology to obtain 3D structures from solid (microcrystalline) samples has recently been developed -- Structure determination is possible -- Nevertheless, amyloids are different -- Isotopic labeling allows to disentangle the intra/inter problem -- HET-s: a functional prion -- Structural information about HET-s (218-289) from earlier measurements -- Chemical shift assignment -- To go further we need distance restraints -- Distance restraints for protein fibrils -- Intramolecular restraints -- Structure calculation -- Structural features of the fibrils -- Comparison with globular proteins.…”
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The structure of amyloid fibrils of the HET-s (218-289) prion as seen by solid-state NMR

Table of Contents: “…Contents: 3D structure is important -- Prion hypothesis -- Prions can form amyloids -- Amyloids -- Cross-beta arrangements give characteristic fiber diffraction patterns -- Solid-state NMR can characterize amyloid fibrils -- Atomic-resolution structure determination by NMR and x-ray -- Distance information in NMR correlation spectra -- The methodology to obtain 3D structures from solid (microcrystalline) samples has recently been developed -- Structure determination is possible -- Nevertheless, amyloids are different -- Isotopic labeling allows to disentangle the intra/inter problem -- HET-s: a functional prion -- Structural information about HET-s (218-289) from earlier measurements -- Chemical shift assignment -- To go further we need distance restraints -- Distance restraints for protein fibrils -- Intramolecular restraints -- Structure calculation -- Structural features of the fibrils -- Comparison with globular proteins.…”
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