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Navigable Slide Index

1. Introduction
2. Topics
3. Prion hypothesis
4. Prions can form amyloids
5. Amyloids (1)
6. Amyloids (2)
7. Amyloids (3)
8. Characteristic fiber diffraction patterns
9. Solid-state NMR can characterize amyloid fibrils
10. Structure determination by NMR and X-ray
11. Distance info in NMR correlation spectra
12. Obtaining sufficient resolution in solid state
13. Atomic-resolution structure determination by NMR
14. Obtain 3D structures from solid samples
15. Several protein structures solved de novo by NMR
16. Heterogeneous samples can not give narrow lines
17. Heterogeneous samples can give narrow lines
18. Comparison of carbon spectra
19. Structure determination possible
20. Nevertheless amyloids are different
21. Isotopic labelling allows to disentangle the problem
22. HET-s: a functional prion
23. The flexible tail forms fibrils
24. Structural information about HET-s (218-289) (1)
25. Structural information about HET-s (218-289) (2)
26. Chemical shift assignment
27. To go further, we need distance restraints
28. Distance restraints for protein fibrils
29. Intramolecular restraints (1)
30. Intramolecular restraints (2)
31. Structure calculation
32. Structural features of the fibrils
33. Fibrils contain a triangular hydrophobic core
34. HET-s(218-289) (1)
35. Overall shape and hydrophobic core
36. Structure stabilized by
37. Structure explains NMR spectra
38. Hydrogen bonds
39. HET-s(218-289) (2)
40. Comparison with globular proteins
41. Outlook
42. 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

Links

Series:

• Prions and Amyloids

Categories:

• Biochemistry
• Methods

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 3, 2024, from https://doi.org/10.69645/LGFT7082.
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Publication History

• Published on September 4, 2008
• Archived on February 25, 2021

Financial Disclosures

• Prof. Beat Meier has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.