• 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. The protein folding problem
3. Thermodynamics
4. Measuring stability
5. Measuring stability using denaturant
6. Stability and unfolding rate of proteins
7. Monitoring of protein folding
8. Measuring change of stability on mutation
9. Kinetics
10. Protein folding landscapes
11. Measuring kinetics
12. Why are ku and kf denaturant dependent
13. The Chevron plot
14. Slopes of the chevron plot and TS structure level
15. Protein engineering - a powerful tool
16. Mapping the transition state - Phi-value analysis
17. Phi-value analysis - free energy dependence
18. Determining changes in free energy
19. Phi value analysis - Phi value = 1
20. Phi value analysis - Phi value = 0
21. Phi value analysis - 0 < Phi < 1
22. Folding of related families of proteins
23. SCOP
24. Folding pathways - constraint by structure
25. Titin I27
26. TI I27 folds via a low energy intermediate
27. TI I27 mutants - Chevron plots
28. Phi value analysis of TI I27
29. Folding rates of other Ig-like proteins
30. All Ig proteins have similar Phi values
31. TI I27 - sturctured TS, TNfn3 - less structured TS
32. TI I27 and spectrin - like proteins
33. TI I27 and spectrin-like proteins - comparison
34. TI I27 and spectrin-like proteins - difference
35. Alpha spectrin-like - folding
36. Folding simulation
37. TI I27 and spectrin-like proteins - conclusion
38. Folding of related protein families - conclusion
39. Acknowledgements

Topics Covered

• The basics of protein folding studies: protein stability (thermodynamics) and protein folding kinetics
• The shape and interpretation of simple chevron plots
• How protein engineering phi value analysis can be used to investigate the structure of the transition state for protein folding
• How studies of the folding of related proteins can simplify the problem of investigating how proteins fold
• Comparison of the folding of complex, all-beta immunoglobulin-like proteins to the folding of simple 3-helix bundles

Links

Series:

• Protein Folding, Aggregation and Design

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Clarke, J. (2007, October 1). Basic studies of protein folding and stability: the folding of related protein families [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 22, 2024, from https://doi.org/10.69645/DUDE7612.
Export Citation (RIS)

Publication History

• Published on October 1, 2007
• Archived on April 17, 2016

Financial Disclosures

• Dr. Jane Clarke has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.