• 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. 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

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.