• 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. Proteins are folded on various scales
3. Proteins are tightly packed
4. Proteins can fold in vivo and in vitro
5. Protein physical properties
6. Calorimetry: experimental test of cooperativity
7. Small proteins are cooperative - two state systems
8. Major insights from theoretical studies
9. Why energy gap is important?
10. A test of protein folding theory
11. Finding folding nucleus in simulations
12. Protein engineering: phi-value analysis
13. Folding nucleus in SH3 domains
14. Evolutionary control of folding rates and stability
15. Evolutionary analysis predicts folding nucleus
16. An all-atom Monte-Carlo folding simulation
17. Protein G-folding: small protein in all-atom detail
18. Protein G folding pathways: summary
19. TSE in protein G
20. A structure belonging to the TSE
21. How to fold a protein: the approach
22. Hydrogen bonding potential
23. Contact term: mu-potential
24. Methods of analysis
25. Folding at physiological temperature
26. Identifying the native state
27. A network ensemble view folding
28. Example: RMSD graph
29. Flux: putting all runs together
30. Summary of folding scenario
31. Atomistically resolved structural intermediate
32. Conclusions

Topics Covered

• Introduction to principles of protein structure
• The basic facts about protein folding
• Cooperativity of protein structure formation
• Necessary and sufficient conditions for protein sequences to fold
• Concept of energy gap
• Protein folding kinetics
• Intermediates and transition state ensembles
• Allatom folding simulations
• Understanding protein folding pathways at atomic detail

Links

Series:

• Protein Folding, Aggregation and Design

Categories:

• Biochemistry

Talk Citation

Publication History

• Published on October 1, 2007

Financial Disclosures

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