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1. Introduction
2. Converting proteins in vitro into amyloid fibrils
3. HypF-N
4. HypF-N forms amyloid fibrils
5. Amyloid formation, a generic property of proteins
6. 3 conformational states of amyloid fibril formation
7. Unfolded systems
8. Unfolding human muscle AcP in 25% TFE
9. The early steps of amyloid formation of AcP
10. The aggregation rates of AcP about 30 mutants
11. Mutations perturbing the rate of aggregation of AcP
12. Aggregation and in hydrophobicity upon mutation
13. Results for mutations in different systems
14. Analysis of mutations of proteins other than AcP
15. Conclusions (1)
16. Hydrophobicity in amyloid fibril formation
17. Net charge in amyloid fibril formation
18. Alpha-helical and beta-sheet propensities
19. Aggregation rate constant
20. Are there sequences that promote aggregation? (1)
21. Are there sequences that promote aggregation? (2)
22. The amino acid sequence of A-beta1-42
23. Strategy
24. Aggregation propensity profile of A-beta
25. Aggregation propensity profile of alpha-synuclein
26. Aggregation propensity profile of PHF43
27. Conclusions (2)
28. Caveats
29. Partially unfolded systems (1)
30. Partially unfolded systems (2)
31. Crucial sequences in the aggregation process
32. A model of the denatured ensemble of AcP
33. The HET-s prion protein from P. anserina (1)
34. The HET-s prion protein from P. anserina (2)
35. Conclusions (3)
36. Do proteins avoid forming misfolded aggregates?
37. Edge beta-strands propagate beta-sheet (1)
38. Strategies used by nature to avoid this process
39. Prevention of aggregation
40. Evolutionary conserved prolines in fibronectin
41. AcP aggregates rapidly if a Gly is substituted
42. Alternating pattern of polar and non-polar residues
43. Natively unfolded proteins remain soluble
44. Suppression of consecutive hydrophobic residues
45. Conclusions (4)
46. Thank you for your kind attention

Topics Covered

• Amyloid fibril formation is a shared property of proteins
• The effect of mutations on the aggregation of unstructured polypeptide chains
• The importance of hydrophobicity, propensity to form beta-sheet structure and charge in amyloid formation of unstructured proteins
• The regions of the sequence forming the beta-core of amyloid fibrils
• The sequence and structural determinants of aggregation for partially folded states of proteins
• Amino acid sequences have evolved to avoid formation of amyloid-like aggregates

Links

Series:

• Protein Folding, Aggregation and Design

Categories:

• Biochemistry

Talk Citation

Chiti, F. (2007, October 1). The sequence determinants of amyloid fibril formation [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 4, 2025, from https://doi.org/10.69645/ZOSY9506.
Export Citation (RIS)

Publication History

• Published on October 1, 2007
• Archived on February 25, 2021

Financial Disclosures

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