• 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. Macromolecular crowding and protein aggregation
3. Topics to be discussed
4. The principle of protein self-assembly
5. Protein binding of a newly synthesized polypeptide
6. Rubisco chloroplast protein
7. Rubisco large subunit binding protein
8. Discovery of the chaperonins
9. BiP binding of the heavy chain of immunoglobulin
10. Origins of the molecular chaperone concept (1)
11. Origins of the molecular chaperone concept (2)
12. The march of molecular chaperones
13. The principle of protein self-assembly
14. In vivo protein folding comparing to in vitro folding
15. Protein aggregation
16. A possible fate for all polypeptide
17. Two key properties
18. Macromolecular crowding
19. Major consequences of macromolecular crowding
20. The excluded volume effect
21. The effect of macromolecular crowding
22. Effects of crowding on reaction rate
23. Predicted effects of macromolecular crowding
24. Effect of crowding agents on refolding of lysozyme
25. Crowding promotes the formation of amyloid fibrils
26. Lysozyme avoid aggregation when folding in ER
27. The solution to aggregation- in small chaperons
28. The solution to aggregation- in large chaperons
29. Molecular chaperones
30. The molecular chaperone function

Topics Covered

• The principle of protein self-assembly
• Discovery of proteins binding to newly synthesized polypeptides
• Discovery of the chaperonins
• Origins of the molecular chaperone concept
• Replacement of spontaneous self-assembly by assisted self-assembly
• Protein aggregation as a universal cellular problem
• Macromolecular crowding and its effects on reaction rates and association constants
• Stimulation of aggregation by crowding
• How chaperones combat aggregation
• Definition of molecular chaperones
• The chaperone function

Links

Series:

• Protein Folding, Aggregation and Design

Categories:

• Biochemistry
• Methods

Talk Citation

Publication History

• Published on October 1, 2007

Financial Disclosures

• Prof. Emeritus R. John Ellis has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.