Key factors in chaperonin-assisted protein folding  

作　　者：Ying Ren Jian Gao ji Xu Wei Ge Jinghai Li 

机构地区：[1]State Key Laboratory of Multiphase Complex System, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China [2]Graduate University of the Chinese Academy of Sciences, Beijing 100039, China

出　　处：《Particuology》2012年第1期105-116,共12页颗粒学报（英文版）

基　　金：supported by National Natural Science Foundation of China under the Grants Nos.20490201 and 20221603;the Ministry of Science and Technology under the grant 2007DFA41320

摘　　要：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 normative proteins fold to their native structures, one of which is the most studied GroELIES 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 200ns 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.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 normative proteins fold to their native structures, one of which is the most studied GroELIES 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 200ns 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.

关 键 词：Molecular dynamics simulationExplicit solventChaperoninProtein folding 

分 类 号：Q51[生物学—生物化学] TG111.4[金属学及工艺—物理冶金]