Explicit solvent molecular dynamics simulations of chaperonin-assisted rhodanese folding--颗粒学报PARTICUOLOGY

Ren, Y., Gao, J., Xu, J., Ge, W., & Li, J. (2009). Explicit solvent molecular dynamics simulations of chaperonin-assisted rhodanese folding. Particuology, 7(3), 220–224. https://doi.org/10.1016/j.partic.2009.03.001

Explicit solvent molecular dynamics simulations of chaperonin-assisted rhodanese folding

Ying Ren ^{a b}, Jian Gao ^a *, Ji Xu ^{a b}, Wei Ge ^a, Jinghai Li ^a

a State Key Laboratory of Multiphase Complex System, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China
b Graduate University of the Chinese Academy of Sciences, Beijing 100039, China

10.1016/j.partic.2009.03.001

Volume 7, Issue 3, June 2009, Pages 220-224

Received 23 December 2008, Accepted 13 March 2009, Available online 15 April 2009.

E-mail: jgao@home.ipe.ac.cn

Highlights

Abstract

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.

Graphical abstract

Keywords

Molecular dynamics simulation; Explicit solvent; Chaperonin-assisted; Protein folding; Molecular chaperonin; Rhodanese

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