Printable Handouts

PDF

Navigable Slide Index

1. Introduction
2. Protein folding
3. Transitions during protein folding
4. Protein folding in the cytosol - evolution
5. The role of mitochondria in protein folding
6. Protein folding in vitro and in mitochondria
7. Aggregation following productive protein folding
8. Interior of a dyctiostelium cell
9. Reconstitution of GroEL-assisted folding
10. Electron micrographs of GroEL
11. Binding of GroES to GroEL
12. GroES and GroEL function as a cage for proteins
13. GroEL mutant Asn229Cys
14. The effect of blocking protein rebinding to GroEL
15. GroEL/GroES accelerates the folding of proteins
16. Proteomic methods to identify GroEL substrates
17. Hsp70 and chaperonins
18. Hsp70 and GroEL/ES roles in protein folding
19. Co-translational chaperoning
20. Nascent chain-binding chaperones
21. Interaction of DnaK with nascent polypeptides
22. Pulse-chase experiments with DnaK
23. Protein folding in the cytosol
24. Structure of prefoldin
25. Hydrophobic patches as sites for substrate binding
26. Can chaperons suppress toxicity of misfolding?
27. Common features of neurodegenerative disorders
28. Amyloid fibrils in neurogenerative diseases
29. Chaperones and the formation of huntingtin fibrils
30. HSP70/40 action on aggregation process
31. Chaperone capacity and misfolded proteins
32. Geldanamycin inhibits huntingtin aggregation

Topics Covered

• The effect of protein aggregation on productive protein folding
• The function of GroEL and GroES as a folding cage for proteins
• Changes in energy landscape within the folding cage
• Cooperation of different chaperone systems in folding pathways: Hsp70 and chaperonins
• Binding of the Hsp70 homologue protein, DnaK, to newly-synthesized polypeptides
• The role of chaperone mechanisms in toxicity suppression of misfolded disease causing proteins
• Potential uses of the chaperone mechanisms in disease therapeutics

Links

Series:

• Molecular Chaperones
• Protein Folding, Aggregation and Design

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Hartl, F.U. (2007, October 1). Chaperone mechanisms in cellular protein folding [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 23, 2024, from https://doi.org/10.69645/PLAP6640.
Export Citation (RIS)

Publication History

• Published on October 1, 2007

Financial Disclosures

• Prof. Dr. F. Ulrich Hartl has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.