• Introduction to Protein Folding and Misfolding
• 69 min
  1. Protein folding and misfolding: from theory to therapy

  • Prof. Christopher Dobson
• Stability and Kinetics of Protein Folding
• 55 min
  2. Mechanisms of protein folding reactions

  • Prof. Thomas Kiefhaber
• Protein Folding Theory
• 53 min
  3. Mapping disordered proteins with single-molecule FRET

  • Dr. Hagen Hofmann
• Protein Folding Simulations
• 36 min
  4. Protein folding

  • Prof. Eugene Shakhnovich
• 42 min
  5. Simulating protein folding with full atomistic detail

  • Prof. Vijay Pande
• 58 min
  6. Molecular dynamics simulations of protein dynamics, unfolding and misfolding

  • Prof. Valerie Daggett
• Protein Folding Inside the Cell: Chaperones
• 42 min
  7. Protein folding Inside the cell: macromolecular crowding and protein aggregation

  • Prof. Emeritus R. John Ellis
• 34 min
  8. Chaperone mechanisms in cellular protein folding

  • Prof. Dr. F. Ulrich Hartl
• 60 min
  9. Quality control of proteins mislocalized to the cytosol

  • Dr. Ramanujan Hegde
• Protein Misfolding and Disease
• 44 min
  10. Protein aggregation, metals and oxidative stress in neurodegenerative diseases

  • Prof. David Allsop
• Protein Design
• 33 min
  11. Designing proteins with life sustaining activities 1

  • Prof. Michael Hecht
• 24 min
  12. Designing proteins with life sustaining activities 2

  • Prof. Michael Hecht
• 48 min
  13. Folding and design of helical repeat proteins

  • Prof. Lynne Regan
• 44 min
  14. Design and engineering of zinc-finger domains

  • Prof. Jacqui Matthews
• 47 min
  15. Prediction and design of protein structures and interactions

  • Prof. David Baker
• Amyloid Fibrils: Structure, Formation and Nanotechnology
• 39 min
  16. Amyloid fibrils as functional nanomaterials

  • Prof. Juliet Gerrard
• 37 min
  17. Functional amyloid fibrils from fungi and viruses

  • Prof. Margaret Sunde
• Intrinsically disordered Proteins
• 40 min
  18. Fuzzy protein theory for disordered proteins

  • Prof. Monika Fuxreiter
• Intersection of RNA, translation and protein aggregation.
• 47 min
  19. Expanding roles of RNA-binding proteins in neurodegenerative diseases

  • Prof. Aaron D. Gitler
• Proteostasis
• 49 min
  20. Adapting proteostasis to ameliorate aggregation-associated amyloid diseases

  • Dr. Jeffery W. Kelly
• Archived Lectures *These may not cover the latest advances in the field
• 60 min
  21. Amyloidosis: disease caused by amyloid

  • Prof. Mark Pepys
• 34 min
  22. Protein folding and dynamics from single molecule spectroscopy

  • Prof. Dr. Benjamin Schuler
• 41 min
  23. Prion diseases

  • Prof. Fred Cohen
• 31 min
  24. Basic studies of protein folding and stability: the folding of related protein families

  • Dr. Jane Clarke
• 38 min
  25. Titin I27: a protein with a complex folding landscape

  • Dr. Jane Clarke
• 49 min
  26. Novel proteins from designed combinatorial libraries

  • Prof. Michael Hecht
• 47 min
  27. Fast folding dynamics of small proteins: placing limits on diffusional limits

  • Dr. Stephen Hagen
• 35 min
  28. The sequence determinants of amyloid fibril formation

  • Prof. Fabrizio Chiti

Printable Handouts

PDF

Navigable Slide Index

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

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.