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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.