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Printable Handouts
Navigable Slide Index
- Introduction
- Protein self assembly and protein aggregation
- Origins of the molecular chaperone concept (1)
- Rubisco: the world's most abundant protein
- Rubisco characteristics
- Rubisco large subunit binding protein
- Discovery of the chaperonins
- Homologues of BiP form the hsp70 family
- Origins of the molecular chaperone concept (2)
- The march of molecular chaperones
- Definition of molecular chaperones
- The molecular chaperone function
- Protein folding in vivo vs. refolding in vitro
- The principles of protein self assembly
- The distinction between folding and assembly
- Assembly chaperones
- Why are chaperones required in the nucleus?
- Effect of nuclear chaperones on nucleosomes
- Structure and assembly of nucleosomes
- Functions and structure of nucleoplasmin
- Model for chaperone function of nucleoplasmin
- Model for chaperone function of GroEL/GroES
- Effect of RbcX on Rubisco in Synechococcus
- RbcX function in cyanobacterial assembly
- Structure of Rubisco L subunit-RbcX complex
Topics Covered
- Definition of protein self-assembly and aggregation
- First use of the term 'molecular chaperone'
- Nucleoplasmin
- Chloroplast rubisco aggregation
- The chaperonins
- The general chaperone concept
- Definition of 'molecular chaperone'
- The chaperone function
- Protein folding on polysomes
- Macromolecular crowding
- Folding and assembly chaperones
- Nuclear chaperones
- Nucleosome assembly
- Mechanism of nucleoplasmin action
- The rubisco assembly chaperone RbcX
Talk Citation
Ellis, R.J. (2007, October 1). History of the molecular chaperone concept: roles in assembly processes [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 3, 2024, from https://doi.org/10.69645/YKNF9012.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Emeritus R. John Ellis has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
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