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1. Introduction
2. Protein folding in vitro
3. Protein folding in vivo
4. Interests
5. Chaperones
6. HdeA protects E. coli from stomach acid
7. E. coli under non-stress conditions
8. HdeA mechanism
9. FRET to monitor HdeA conformation
10. HdeA unfolding monitored by FRET
11. HdeA adaptively binds substrates
12. HdeA releases substrates very slowly
13. Monitoring structural changes in HdeA
14. Examine HdeA
15. Examine substrate
16. In vivo folding
17. Ways to measure folding and stability
18. To better understand in vivo folding
19. A tripartite fusion system
20. Quantitative in vivo stability readout
21. Proteins inserted into beta-lactamase
22. Selection for stabilized IM7 variants
23. PenV-resistant IM7 mutants are stabilized
24. Most proteins are only marginally stable
25. Why are proteins so unstable?
26. Stabilizing mutations map to binding interface
27. Optimizing folding in vivo
28. A dual selection system
29. Effect instability of the inserted protein
30. Fold or die!
31. IM7 and Spy in the periplasm of EMS strains
32. BaeS regulates Spy
33. Spy overproduction is sufficient to stabilize IM7
34. Spy inhibits MDH aggregation
35. Spy suppresses protein aggregation
36. Spy enhances protein refolding
37. Spy and tannins
38. Spy forms a thin cradle shaped dimer
39. Substrate binding and environment changes
40. Optimization of in vivo folding
41. Acknowledgments

Topics Covered

• Protein folding in vivo
• Protein folding as facilitated by the acid inducible chaperone HdeA
• Optimization of folding in vivo illustrates a tradeoff between stability and function
• The Spy chaperone

Links

Series:

• Protein Homeostasis

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Publication History

• Published on February 2, 2012

Financial Disclosures

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