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
β¦ LIBER β¦
Local Interactions Dominate Folding in a Simple Protein Model
β Scribed by Ron Unger; John Moult
- Book ID
- 115627432
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 230 KB
- Volume
- 259
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
A simple model of chaperonin-mediated pr
β
Chan, Hue Sun; Dill, Ken A.
π
Article
π
1996
π
John Wiley and Sons
π
English
β 678 KB
Protein Folding: Simple Models for a Com
β
Amedeo Caflisch
π
Article
π
2004
π
Elsevier Science
π
English
β 101 KB
Compacting local protein folds with a βh
β
A. G. de Brevern; S. Hazout
π
Article
π
2001
π
Springer
π
English
β 491 KB
Nonadditive Interactions in Protein Fold
β
A. N. Morozov; Y. J. Shiu; C. T. Liang; M. Y. Tsai; S. H. Lin
π
Article
π
2007
π
Springer Netherlands
π
English
β 313 KB
Entropy in protein folding and in protei
β
G Patrick Brady; Kim A Sharp
π
Article
π
1997
π
Elsevier Science
π
English
β 671 KB
Folding of proteins in Go models with an
β
Marek Cieplak; Trinh Xuan Hoang
π
Article
π
2003
π
Elsevier Science
π
English
β 292 KB
Molecular dynamics studies of Go models of proteins with the 10 -12 contact potential and the bond and dihedral angle terms indicate statistical similarities to other Go models, e.g., with the Lennard-Jones contact potentials. The folding times depend on the protein size as power laws with the expon