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Navigable Slide Index

1. Introduction
2. Talk outline
3. From DNA to a folded protein
4. Protein folding - Anfinsen
5. Spontaneous or assisted folding?
6. Folding inside the mitochondria
7. Infinite reflections? Ming Cheng - circa 1989
8. A visit to the black forest
9. Origin of the chaperonins - GP1
10. Archaea
11. TF55 and GroEL
12. Origin of the chaperonins
13. Reconstitution
14. Chaperonins provide kinetic assistance
15. Collaborating with Paul Sigler
16. Kerstin Braig and her crystals of GroEL
17. A model of GroEL
18. Polypeptide binding
19. Substrate polypeptide binds to multiple domains
20. Rescue of kinetically-trapped monomer
21. Using labeled DHFR
22. Binding as a means of rescue
23. Rescue of rubisco by binding to GroEL

Topics Covered

• Chaperonin-mediated protein folding by GroEL/GroES
• Folding of newly-translated protein
• Currently known Molecular chaperones (including the Heat shock protein Hsp group)
• Recognition of non native proteins by Hsps and formation of aggregates
• Aggregates and neurodegenerative disease -The discovery of the chaperonin-mediated folding
• The structure of the GroES/GroeEL chaperonin class of molecular chaperones
• The steps of polypeptide binding and folding
• The action of ATP binding and hydrolysis in driving the rings of the machine through cycles of binding and release cycle

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Categories:

• Biochemistry

Talk Citation

Publication History

• Published on September 10, 2012

Financial Disclosures

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