Explicit solvent molecular dynamics simulations of chaperonin-assisted rhodanese folding
✍ Scribed by Ying Ren; Jian Gao; Ji Xu; Wei Ge; Jinghai Li
- Publisher
- Elsevier
- Year
- 2009
- Tongue
- English
- Weight
- 687 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1674-2001
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✦ Synopsis
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 performed for the first time on rhodanese folding in a series of cavity-size and cavity-charge chaperonin mutants. A compromise between stability and flexibility of chaperonin structure during the substrate folding has been observed and the key factors affecting this dynamic process are discussed.