Registration for a live webinar on 'Innovative Vaccines and Viral Pathogenesis: Insights from Recent Monkeypox (Mpox) Research' is now open.
See webinar detailsWe noted you are experiencing viewing problems
-
Check with your IT department that JWPlatform, JWPlayer and Amazon AWS & CloudFront are not being blocked by your network. The relevant domains are *.jwplatform.com, *.jwpsrv.com, *.jwpcdn.com, jwpltx.com, jwpsrv.a.ssl.fastly.net, *.amazonaws.com and *.cloudfront.net. The relevant ports are 80 and 443.
-
Check the following talk links to see which ones work correctly:
Auto Mode
HTTP Progressive Download Send us your results from the above test links at access@hstalks.com and we will contact you with further advice on troubleshooting your viewing problems. -
No luck yet? More tips for troubleshooting viewing issues
-
Contact HST Support access@hstalks.com
-
Please review our troubleshooting guide for tips and advice on resolving your viewing problems.
-
For additional help, please don't hesitate to contact HST support access@hstalks.com
We hope you have enjoyed this limited-length demo
This is a limited length demo talk; you may
login or
review methods of
obtaining more access.
Printable Handouts
Navigable Slide Index
- Introduction
- The protein folding problem
- Thermodynamics
- Measuring stability
- Measuring stability using denaturant
- Stability and unfolding rate of proteins
- Monitoring of protein folding
- Measuring change of stability on mutation
- Kinetics
- Protein folding landscapes
- Measuring kinetics
- Why are ku and kf denaturant dependent
- The Chevron plot
- Slopes of the chevron plot and TS structure level
- Protein engineering - a powerful tool
- Mapping the transition state - Phi-value analysis
- Phi-value analysis - free energy dependence
- Determining changes in free energy
- Phi value analysis - Phi value = 1
- Phi value analysis - Phi value = 0
- Phi value analysis - 0 < Phi < 1
- Folding of related families of proteins
- SCOP
- Folding pathways - constraint by structure
- Titin I27
- TI I27 folds via a low energy intermediate
- TI I27 mutants - Chevron plots
- Phi value analysis of TI I27
- Folding rates of other Ig-like proteins
- All Ig proteins have similar Phi values
- TI I27 - sturctured TS, TNfn3 - less structured TS
- TI I27 and spectrin - like proteins
- TI I27 and spectrin-like proteins - comparison
- TI I27 and spectrin-like proteins - difference
- Alpha spectrin-like - folding
- Folding simulation
- TI I27 and spectrin-like proteins - conclusion
- Folding of related protein families - conclusion
- Acknowledgements
Topics Covered
- The basics of protein folding studies: protein stability (thermodynamics) and protein folding kinetics
- The shape and interpretation of simple chevron plots
- How protein engineering phi value analysis can be used to investigate the structure of the transition state for protein folding
- How studies of the folding of related proteins can simplify the problem of investigating how proteins fold
- Comparison of the folding of complex, all-beta immunoglobulin-like proteins to the folding of simple 3-helix bundles
Talk Citation
Clarke, J. (2007, October 1). Basic studies of protein folding and stability: the folding of related protein families [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 23, 2024, from https://doi.org/10.69645/DUDE7612.Export Citation (RIS)
Publication History
Financial Disclosures
- Dr. Jane Clarke has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Basic studies of protein folding and stability: the folding of related protein families
A selection of talks on Biochemistry
Hide