The interaction network of the GroEL chaperonin
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| Format: | Electronic |
| Language: | English |
| Published: |
London :
Henry Stewart Talks,
2012.
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| Series: | Henry Stewart talks. Biomedical & life sciences collection. Protein homeostasis.
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| Subjects: | |
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Table of Contents:
- Contents: De novo protein folding and proteome maintenance critically depend on molecular chaperones
- Transitions during protein folding
- Chaperone assisted protein folding
- Productive protein folding is often competed by aggregation
- Reconstitution of GroEL-assisted folding
- GroEL and GroES function as a folding cage for proteins up to 60 kDa
- GroEL structure
- Which proteins need GroEL/GroES for folding?
- Identification of the GroEL interaction proteome
- Class III substrates are of relatively low cellular abundance but occupy most of the GroEL capacity
- Chaperonins provide a specialized folding environment with two functional elements: sequestration and steric confinement in a hydrophilic cage
- GroEL as part of the cytosolic chaperone network.