• Overview of Molecular Chaperones
• 34 min
  1. History of the molecular chaperone concept: roles in assembly processes

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

  • Prof. Dr. F. Ulrich Hartl
• Prokaryotic Molecular Chaperones
• 38 min
  3. Mechanistic aspects of chaperonin GroEL/ES function

  • Prof. Amnon Horovitz
• 99 min
  4. Structure and function of the ATP-dependent Clp chaperone/protease machines

  • Dr. Michael R. Maurizi
• 32 min
  5. The role of chaperones and Sec machinery in protein secretion

  • Prof. Koreaki Ito
• 44 min
  6. How can molecular chaperones repair damaged protein structures?

  • Prof. Pierre Goloubinoff
• 32 min
  7. Disulfide bond formation in vivo

  • Prof. James Bardwell
• Eukaryotic Molecular Chaperones
• 39 min
  8. Overview of eukaryotic molecular chaperones in the cytosol

  • Dr. Jason C. Young
• 36 min
  9. Chaperonin-containing TCP-1 (CCT), actin springs, and protein folding fluxes

  • Prof. Keith Willison
• 35 min
  10. The functions of the Hsp70 system

  • Prof. Jeffrey L. Brodsky
• 26 min
  11. Hsp90: a chaperone for protein kinases and hormone receptors

  • Dr. David Toft
• Role of Chaperones in Diseases
• 38 min
  12. The roles of molecular chaperones in bacterial infection

  • Prof. Tomoko Yamamoto
• 46 min
  13. Role of chaperonin-like proteins in Bardet-Biedl syndrome

  • Dr. Michel R. Leroux
• 53 min
  14. Roles for molecular chaperones in cystic fibrosis

  • Prof. Douglas M. Cyr
• 51 min
  15. Targeting cancer: designing drugs against Hsp90

  • Dr. Gabriela Chiosis
• Archived Lectures *These may not cover the latest advances in the field
• 29 min
  16. Overview of prokaryotic molecular chaperones

  • Prof. Walid A. Houry
• 47 min
  17. The biogenesis of E. coli inner membrane proteins

  • Dr. Joen Luirink
• 39 min
  18. Mechanism of chaperone action of small heat shock proteins

  • Prof. Elizabeth Vierling
• 22 min
  19. ClpB: a chaperone for protein disaggregation

  • Prof. Michal Zolkiewski
• 38 min
  20. The roles of chaperonins in bacteria

  • Dr. Peter Lund
• 44 min
  21. Towards a unifying mechanism for the Hsp70 chaperones

  • Prof. Pierre Goloubinoff
• 29 min
  22. Adaptor mediated activation of the Hsp100/ Clp protein ClpC controls general and regulatory proteolysis in Bacillus subtilis

  • Prof. Dr. Kursad Turgay
• 33 min
  23. Hsp31: a general stress protein of Escherichia coli

  • Prof. Francois Baneyx
• 46 min
  24. Hsp104: a specialized chaperone for protein disaggregation

  • Dr. John R. Glover
• 47 min
  25. Molecular chaperones and handling of abnormal proteins in neurodegenerative disorders

  • Prof. Michael Sherman
• 20 min
  26. The role of chaperones in Parkinson's disease

  • Dr. Konstanze F. Winklhofer

Printable Handouts

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Navigable Slide Index

1. Introduction
2. Disulfide bond formation is an oxidation reaction
3. Importance of disulfide bonds
4. Disulfide bonds are formed in E. coli periplasm
5. Chris Anfinsen and thermodynamic hypothesis
6. De novo disulfide formation in E. coli periplasm
7. The secretory pathway
8. Disulfide bonds formation by ER thiol oxidases
9. A model for QSOX-PDI cooperation
10. Eukaryotic/prokaryotic disulfide bond formation
11. A new pathway for disulfide bond formation
12. DsbA and thioredoxin are structurally related
13. DsbA and DsbB deletion and replacement
14. Producing more oxidizing thioredoxin mutants
15. Motility requires disulfide bonds
16. 2 mutants can partially rescue dsb- phenotype
17. Mutant protein is brown
18. Absorbance spectrum CACC
19. Iron-sulfur clusters
20. Mutant thioredoxin's properties
21. Mutant has two exposed cysteines
22. Replacing normal pathway with a new pathway
23. DsbB's quinone reductase activity
24. Current model for the mechanism of DsbB
25. Kinetics of the DsbB reaction
26. Single wavelength kinetic measurement
27. k1 depends on DsbA concentration
28. k2 is fairly DsbA independent
29. Kinetic measurements at 275 nm
30. Kinetic scheme for DsbB reaction cycle
31. Disulfide bond formation in prokaryotes
32. Alchemy
33. E. coli - the modern alchemist
34. De novo disulfide formation and isomerization
35. What distinguishes DsbC from DsbG?
36. Annie Hiniker
37. dsbC null mutants are copper sensitive
38. WT DsbG doesn't rescue dsbC- Cu sensitivity
39. Evolution of DsbG so it functions as DsbC
40. DsbG K113E reverses electrostatic charge
41. DsbG V216M mutant alters alpha c loop position
42. DsbG V216M mutant reverses charge
43. Acidic patch mutations in lysine 113
44. Summary

Topics Covered

• Disulfide bond formation in prokaryotes
• In eukaryotes
• An engineered pathway
• DsbB, the source of disulfides
• Disulfide isomerases

Links

Series:

• Molecular Chaperones

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Publication History

• Published on October 1, 2007

Financial Disclosures

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