Molecular Dynamic Simulation of Chaperonin-Mediated Protein Folding
โ Scribed by Yan Cui; Run Sheng Chen; Wing Hung Wong
- Book ID
- 110421028
- Publisher
- Springer
- Year
- 1998
- Tongue
- English
- Weight
- 315 KB
- Volume
- 17
- Category
- Article
- ISSN
- 1573-4943
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Chaperonins are known to facilitate the productive folding of numerous misfolded proteins. Despite their established importance, the mechanism of chaperonin-assisted protein folding remains unknown. In the present article, all-atom explicit solvent molecular dynamics (MD) simulations have been perfo
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
Molecular dynamics (MD) is an invaluable tool with which to study protein folding in silico. Although just a few years ago the dynamic behavior of a protein molecule could be simulated only in the neighborhood of the experimental conformation (or protein unfolding could be simulated at high temperat