Thermal Unfolding of a Double-Domain Protein: Molecular Dynamics Simulation of Rhodanese
文献类型：期刊论文
| 作者 | Ren, Ying1,2; Gao, Jian1; Ge, Wei1; Li, Jinghai1 |
| 刊名 | INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH
 |
| 出版日期 | 2009-10-07 |
| 卷号 | 48期号:19页码:8865-8871 |
| 关键词 | BOVINE LIVER RHODANESE LINEAR CONSTRAINT SOLVER C-TERMINAL DOMAIN ARTIFICIAL PERIODICITY DENATURED RHODANESE FOLDING PATHWAY ACTIVE-SITE UREA INTERMEDIATE TEMPERATURE |
| ISSN号 | 0888-5885 |
| 通讯作者 | Ren, Y |
| 英文摘要 | The thermal unfolding process of bovine liver rhodanese, composing two globular domains (N-domain and C-domain) with similar tertiary structures, has been studied by explicit solvent molecular dynamics (MD) simulations at high temperatures of 450 and 500 K, as well as 308 K for comparisons. The results are in good agreement with the available experimental results (Horowitz, P. M.; Butler, M. Interactive Intermediates Are Formed During the Urea Unfolding of Rhodariese. J. Biol. Chem. 1993, 268 (4), 2500-2504. Shibatani, T.; Kramer, G.; Hardesty, B.; Horowitz, P. M. Domain Separation Precedes Global Unfolding of Rhodanese. J. Biol. Chem. 1999, 274 (47), 33795-33799. Ybarra, J.; Bhattacharyya, A. M.; Panda, M.; Horowitz, P. M, Active Rhodanese Lacking Nonessential Sulfhydryl Groups Contains an Unstable C-Terminal Domain and Can Be Bound, Inactivated, and Reactivated by GroEL..J. Biol. Chem. 2003, 278 (3), 1693-1699). Besides that our simulation can also depict more dynamic details of the unfolding process. The solvent accessible surface area (SASA) shows a remarkable increase mainly due to a more exposed hydrophobic area, indicating that the hydrophobic interaction is considerably weaker at high temperatures. Comparisons between the thermal stabilities of equivalent secondary structures in both domains suggest that the C-domain is more fragile than the N-domain and the breaking down of the secondary structures follows the pattern [alpha-helix]->[bend, turn, 3-helix, and 5-helix]. Different regimes of unfolding intermediates have also been discussed. |
| WOS标题词 | Science & Technology ; Technology |
| 类目[WOS] | Engineering, Chemical |
| 研究领域[WOS] | Engineering |
| 关键词[WOS] | BOVINE LIVER RHODANESE ; LINEAR CONSTRAINT SOLVER ; C-TERMINAL DOMAIN ; ARTIFICIAL PERIODICITY ; DENATURED RHODANESE ; FOLDING PATHWAY ; ACTIVE-SITE ; UREA ; INTERMEDIATE ; TEMPERATURE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000270362500012 |
| 公开日期 | 2013-11-29 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/6568]  |
| 专题 | 过程工程研究所_多相复杂系统国家重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, State Key Lab Multiphase Complex Syst, Inst Proc Engn, Beijing 100190, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China |
| 推荐引用方式 GB/T 7714 | Ren, Ying,Gao, Jian,Ge, Wei,et al. Thermal Unfolding of a Double-Domain Protein: Molecular Dynamics Simulation of Rhodanese[J]. INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH,2009,48(19):8865-8871. |
| APA | Ren, Ying,Gao, Jian,Ge, Wei,&Li, Jinghai.(2009).Thermal Unfolding of a Double-Domain Protein: Molecular Dynamics Simulation of Rhodanese.INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH,48(19),8865-8871. |
| MLA | Ren, Ying,et al."Thermal Unfolding of a Double-Domain Protein: Molecular Dynamics Simulation of Rhodanese".INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH 48.19(2009):8865-8871. |
入库方式： OAI收割
来源：过程工程研究所
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