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1. Introduction
2. The protein folding process
3. The cytoplasm is very crowded and viscous
4. Proteins are not very stable
5. Concept of a molecular chaperone
6. Chaperones in E. coli
7. Chaperones to be discussed
8. Chaperones and biosynthesis in E. coli
9. Trigger factor
10. Structure of E. coli trigger factor
11. Structure of E. coli TF bound to ribosome
12. The cradle model of TF function
13. The dynamic cycling model for TF function
14. The Hsp70/Hsp40 chaperone system
15. E. coli DnaK/DnaJ/GrpE structures
16. DnaK/DnaJ/GrpE functional cycle
17. Evidence for the K/J/E cycle from structural data
18. Motifs bound by DnaK and DnaJ
19. GroEL/GroES system
20. GroEL/GroES structure before and after binding
21. GroEL apical domain is implicated in binding
22. Mechanism used by GroEL in protein binding
23. GroEL cycle
24. GroEL function in vivo
25. The Clp ATPases
26. ClpB as a protein disaggregation machine
27. ClpXP complex model structure
28. Substrates of ClpXP
29. SsrA targets unfinished proteins for proteolysis
30. ClpXP mechanism of function
31. Model for substrate entry and product release
32. Conclusion

Topics Covered

• Protein folding in vitro versus in vivo
• Concept of a molecular chaperone
• Chaperones in E. coli
• Trigger factor
• DnaK/DnaJ/GrpE system
• GroEL/GroES system
• Clp ATPases

Links

Series:

• Molecular Chaperones

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Publication History

• Published on October 1, 2007
• Archived on August 13, 2020

Financial Disclosures

• Prof. Walid A. Houry has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.