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Printable Handouts
Navigable Slide Index
- Introduction
- Protein folding in vitro
- Protein folding in vivo
- Interests
- Chaperones
- HdeA protects E. coli from stomach acid
- E. coli under non-stress conditions
- HdeA mechanism
- FRET to monitor HdeA conformation
- HdeA unfolding monitored by FRET
- HdeA adaptively binds substrates
- HdeA releases substrates very slowly
- Monitoring structural changes in HdeA
- Examine HdeA
- Examine substrate
- In vivo folding
- Ways to measure folding and stability
- To better understand in vivo folding
- A tripartite fusion system
- Quantitative in vivo stability readout
- Proteins inserted into beta-lactamase
- Selection for stabilized IM7 variants
- PenV-resistant IM7 mutants are stabilized
- Most proteins are only marginally stable
- Why are proteins so unstable?
- Stabilizing mutations map to binding interface
- Optimizing folding in vivo
- A dual selection system
- Effect instability of the inserted protein
- Fold or die!
- IM7 and Spy in the periplasm of EMS strains
- BaeS regulates Spy
- Spy overproduction is sufficient to stabilize IM7
- Spy inhibits MDH aggregation
- Spy suppresses protein aggregation
- Spy enhances protein refolding
- Spy and tannins
- Spy forms a thin cradle shaped dimer
- Substrate binding and environment changes
- Optimization of in vivo folding
- 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
Talk Citation
Bardwell, J. (2012, February 2). Protein folding in vivo [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 14, 2024, from https://doi.org/10.69645/BSRG3625.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. James Bardwell has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.