Molecular Docking and Dynamics Simulation Improving Thermophilic Protease Activity of PhpI
文献类型：期刊论文
| 作者 | Zhan DL ; Gao N ; Han WW ; Feng Y |
| 刊名 | chemical journal of chinese universities-chinese
 |
| 出版日期 | 2013 |
| 卷号 | 34期号:3页码:628-633 |
| 关键词 | ESCHERICHIA-COLI HSP31 CRYSTAL-STRUCTURE CHAPERONE RESOLUTION DJ-1 |
| ISSN号 | 0251-0790 |
| 通讯作者 | han ww |
| 中文摘要 | in this study, flexible docking approach was employed to dock the substrate into the active site of protease ph1704 (phpi), combining with crystal structure to determine the key enzyme, and study on site-mutation in theroy. all parameters were verified by molecular biology experiment. the protease activity of k43c was 5. 8 times higher than that of wt. molecular dynamics simulation reveals that after 8 ns dynamics simulations, the secondary structure of 1(43c mutant changes from the s2 sheet of wt(f11-e12-d13) to the loop. k43 and e12 are both the important active site residues. the change will enhance the flexibility of active site, and be helpful for catalytic reactions. the new structural and mechanistic insights obtained from molecular docking and dynamics simulation should be valuable for detailed researching of structures and mechanisms of the member of the dj-1 superfamily. |
| 收录类别 | SCI收录期刊论文 |
| 语种 | 中文 |
| WOS记录号 | WOS:000317085500025 |
| 公开日期 | 2014-04-16 |
| 源URL | [http://ir.ciac.jl.cn/handle/322003/49984]  |
| 专题 | 长春应用化学研究所_长春应用化学研究所知识产出_期刊论文 |
| 推荐引用方式 GB/T 7714 | Zhan DL,Gao N,Han WW,et al. Molecular Docking and Dynamics Simulation Improving Thermophilic Protease Activity of PhpI[J]. chemical journal of chinese universities-chinese,2013,34(3):628-633. |
| APA | Zhan DL,Gao N,Han WW,&Feng Y.(2013).Molecular Docking and Dynamics Simulation Improving Thermophilic Protease Activity of PhpI.chemical journal of chinese universities-chinese,34(3),628-633. |
| MLA | Zhan DL,et al."Molecular Docking and Dynamics Simulation Improving Thermophilic Protease Activity of PhpI".chemical journal of chinese universities-chinese 34.3(2013):628-633. |
入库方式： OAI收割
来源：长春应用化学研究所
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