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Printable Handouts
Navigable Slide Index
- Introduction
- Topics
- Prion hypothesis
- Prions can form amyloids
- Amyloids (1)
- Amyloids (2)
- Amyloids (3)
- Characteristic fiber diffraction patterns
- Solid-state NMR can characterize amyloid fibrils
- Structure determination by NMR and X-ray
- Distance info in NMR correlation spectra
- Obtaining sufficient resolution in solid state
- Atomic-resolution structure determination by NMR
- Obtain 3D structures from solid samples
- Several protein structures solved de novo by NMR
- Heterogeneous samples can not give narrow lines
- Heterogeneous samples can give narrow lines
- Comparison of carbon spectra
- Structure determination possible
- Nevertheless amyloids are different
- Isotopic labelling allows to disentangle the problem
- HET-s: a functional prion
- The flexible tail forms fibrils
- Structural information about HET-s (218-289) (1)
- Structural information about HET-s (218-289) (2)
- Chemical shift assignment
- To go further, we need distance restraints
- Distance restraints for protein fibrils
- Intramolecular restraints (1)
- Intramolecular restraints (2)
- Structure calculation
- Structural features of the fibrils
- Fibrils contain a triangular hydrophobic core
- HET-s(218-289) (1)
- Overall shape and hydrophobic core
- Structure stabilized by
- Structure explains NMR spectra
- Hydrogen bonds
- HET-s(218-289) (2)
- Comparison with globular proteins
- Outlook
- Acknowledgement
Topics Covered
- 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
Talk Citation
Meier, B. (2008, September 4). The structure of amyloid fibrils of the HET-s (218-289) prion as seen by solid-state NMR [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 12, 2024, from https://doi.org/10.69645/LGFT7082.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Beat Meier has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
The structure of amyloid fibrils of the HET-s (218-289) prion as seen by solid-state NMR
A selection of talks on Biochemistry
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