Chaperonins are oligomeric proteins that help other proteins fold. They act, according to the "Anfinsen cage" or "box of infinite dilution" model, to provide private space, protected from aggregation, where a protein can fold. Recent evidence indicates, however, that proteins are often ejected from
GroEL—GroES-Mediated Protein Folding
✍ Scribed by Arthur L. Horwich; George W. Farr; Wayne A. Fenton
- Publisher
- John Wiley and Sons
- Year
- 2006
- Weight
- 8 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0931-7597
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A mechanism for heavy chain binding protein (BiP)-and protein disul"de isomerase (PDI)mediated protein folding and assembly has been proposed. It considers BiP chaperoning action and PDI catalytic activity. A kinetic model has been developed based on the proposed mechanism. The model was used for qu
The most surprising feature of proteins, which distinguishes them from all other types of large polymeric molecules and provides them with a broad range of special properties, is their unique structural order. The position of each atom in these macromolecules is unique relative to its neighboring at
An important idea that emerges from the energy landscape theory of protein folding is that subtle global features of the protein landscape can profoundly affect the apparent mechanism of folding. The relationship between various characteristic temperatures in the phase diagrams and landmarks in the