Key factors in chaperonin-assisted protein folding--颗粒学报PARTICUOLOGY

Ren, Y., Gao, J., Xu, J., Ge, W., & Li, J. (2012). Key factors in chaperonin-assisted protein folding. Particuology, 10(1), 105–116. https://doi.org/10.1016/j.partic.2011.02.011

Key factors in chaperonin-assisted protein folding

Ying Ren ^a *, 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.2011.02.011

Volume 10, Issue 1, February 2012, Pages 105-116

Received 14 July 2010, Revised 11 February 2011, Accepted 17 February 2011, Available online 28 January 2012.

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

Highlights

Abstract

Incorrect folding of proteins in the macromolecular crowding environment in living cells would cause cellular disasters. All cells have developed their structurally and functionally distinct classes of molecular chaperones to help nonnative proteins fold to their native structures, one of which is the most studied GroEL/ES complex. In the present article, large-scale all-atom explicit solvent molecular dynamics (MD) simulations have been carried out on rhodanese folding in a series of chaperonin mutants for 200 ns to understand the mechanism therein. In accordance with experimental results, two factors have been identified to play a significant role, the geometrical confinement effect of the folding cavity and the charge effect of the inner surface of the cavity. Our analysis of the properties during simulation suggests that the GroEL/ES complex directly exerts force on the contacting residues of the substrate, thus assists substrate folding.

Graphical abstract

Keywords

Molecular dynamics simulation; Explicit solvent; Chaperonin; Protein folding

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