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1. Introduction
2. The significance of proteins
3. The structure of proteins
4. Protein folding
5. Protein complexity
6. Folding and self-assembly is the essence of life
7. Folding in a cellular environment
8. What are the underlying principles of folding?
9. Distributions of conformations
10. A simple energy surface for protein folding
11. Mutational studies of acylphosphatase
12. Structure of the transition state ensemble
13. Native and transition states of acylphosphatase
14. The transition state of an SH3 domain
15. Exploring the energy surface
16. NMR relaxation dispersion
17. Intermediates of mutational variants
18. Energetic of the folding process
19. Probing different regions of the surface
20. The folding of lysozyme
21. Mapping the energy surface of lysozyme
22. A general mechanism of folding
23. What are the consequences of protein misfolding?
24. Folding and cell biology
25. Relationship between folding and disease
26. Protein deposition diseases
27. Protein aggregates formed in amyloid diseases
28. Protein deposition in a systemic amyloidosis
29. Amyloidogenic mutation of lysozyme
30. Amyloid fibrils from Asp67His lysozyme
31. Mechanism of amyloid formation
32. Structure of the amyloidogenic intermediate
33. Schematic energy surface for lysozyme
34. Amyloid formation by lysozyme in vivo
35. The design of an aggregation inhibitor
36. Crystal structure of the complex
37. Towards novel therapeutic strategies
38. Protein amyloid diseases
39. Why do proteins convert into amyloid fibrils?
40. SH3 domain of PI3 kinase
41. Electron microscopy of the SH3 gel
42. Higher resolution image of an amyloid fibril
43. Model of an amyloid fibril
44. NMR structure of a peptide in a fibril
45. X-ray structure of a fibrillar peptide
46. The generic nature of amyloid fibrils
47. Multiple states accessible to a polypeptide chain
48. Representative protein folds
49. Myoglobin fibrils
50. Fibrils from homopolymers
51. Protein are evolved polymers
52. Multiple states accessible to a polypeptide chain
53. Mutational effects on aggregation rates
54. What are the underlying origins of amyloid disease?
55. Biological control of protein folding and assembly
56. Generic toxicity of amyloid aggregates
57. Cellular defences against aggregation
58. Limitations of molecular evolution
59. Evolution of cellular organisation
60. "Post evolutionary" diseases
61. Defining complete "energy landscapes" for proteins
62. Misfolding diseases: therapeutic strategies
63. Opportunities for the future
64. Acknowledgements
65. Principal funding sources

Topics Covered

• Protein nature, folding and complexity
• Folding in a cellular environment
• The underlying principles of folding
• Native and transition states
• Exploring the energy surface
• The folding of lysozyme
• The consequences of protein misfolding
• The relationship between folding and disease
• Protein deposition diseases
• Protein aggregates in amyloid diseases
• Amyloidogenic mutations of lysozyme
• Mechanism of amyloid formation
• Structure of the amyloidogenic intermediate
• Amyloid formation by lysozyme in vivo
• SH3 domain of PI3 kinase
• Model of an amyloid fibril
• The underlying origins of amyloid disease
• Generic toxicity of amyloid aggregates
• Cellular defences against aggregation
• Evolutionary design of proteins
• "Post-evolutionary" diseases

Links

Series:

• Protein Folding, Aggregation and Design

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Dobson, C. (2007, October 1). Protein folding and misfolding: from theory to therapy [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved April 15, 2025, from https://doi.org/10.69645/FXWP4611.
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Publication History

• Published on October 1, 2007

Financial Disclosures

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