COMPARING FOLDING MECHANISMS OF DIFFERENT PRION PROTEINS BY G(o)over-bar MODEL
文献类型：期刊论文
| 作者 | Wu, Xue1,2,3; Fu, Ting1,2,3; Xiu, Zhi-Long1; Yin, Liu4; Wang, Jin-Guang5; Li, Guo-Hui2 |
| 刊名 | journal of theoretical & computational chemistry
 |
| 出版日期 | 2013-12-01 |
| 卷号 | 12期号:8 |
| 关键词 | Prion protein fold Go model cooperativity stability |
| 英文摘要 | prions are associated with neurodegenerative diseases induced by transmissible spongiform encephalopathies. the infectious scrapie form is referred to as prpsc, which has conformational change from normal prion with predominant alpha-helical conformation to the abnormal prpsc that is rich in beta-sheet content. neurodegenerative diseases have been found from both human and bovine sources, but there are no reports about infected by transmissible spongiform encephalopathies from rabbit, canine and horse sources. here we used coarse-grained g (o) over bar model to compare the difference among human, bovine, rabbit, canine, and horse normal (cellular) prion proteins. the denatured state of normal prion has relation with the conversion from normal to abnormal prion protein, so we used all-atom g (o) over bar model to investigate the folding pathway and energy landscape for human prion protein. through using coarse-grained g (o) over bar model, the cooperativity of the five prion proteins was characterized in terms of calorimetric criterion, sigmoidal transition, and free-energy profile. the rabbit and horse prion proteins have higher folding free-energy barrier and cooperativity, and canine prion protein has slightly higher folding free-energy barrier comparing with human and bovine prion proteins. the results from all-atom go model confirmed the validity of c-alpha-g (o) over bar model. the correlations of our results with previous experimental and theoretical researches were discussed. |
| WOS标题词 | science & technology ; physical sciences |
| 类目[WOS] | chemistry, multidisciplinary |
| 研究领域[WOS] | chemistry |
| 关键词[WOS] | molecular-dynamics simulations ; free-energy calculations ; structural stability ; contact order ; nmr structure ; domain prp(121-231) ; hiv-1 protease ; scrapie ; cooperativity ; transition |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000328359500004 |
| 公开日期 | 2015-11-10 |
| 源URL | [http://159.226.238.44/handle/321008/137653]  |
| 专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
| 作者单位 | 1.Dalian Univ Technol, Sch Life Sci & Biotechnol, Dalian 116024, Peoples R China 2.Chinese Acad Sci, Lab Mol Modeling & Design, State Key Lab Mol React Dynam, Dalian Inst Chem Phys, Dalian, Liaoning, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 4.Dalian Med Univ, Affiliated Hosp 1, Dept Oncol, Dalian 116011, Liaoning Provin, Peoples R China 5.Dalian Med Univ, Affiliated Hosp 1, Dept Thorac Surg, Dalian 116011, Liaoning Provin, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wu, Xue,Fu, Ting,Xiu, Zhi-Long,et al. COMPARING FOLDING MECHANISMS OF DIFFERENT PRION PROTEINS BY G(o)over-bar MODEL[J]. journal of theoretical & computational chemistry,2013,12(8). |
| APA | Wu, Xue,Fu, Ting,Xiu, Zhi-Long,Yin, Liu,Wang, Jin-Guang,&Li, Guo-Hui.(2013).COMPARING FOLDING MECHANISMS OF DIFFERENT PRION PROTEINS BY G(o)over-bar MODEL.journal of theoretical & computational chemistry,12(8). |
| MLA | Wu, Xue,et al."COMPARING FOLDING MECHANISMS OF DIFFERENT PRION PROTEINS BY G(o)over-bar MODEL".journal of theoretical & computational chemistry 12.8(2013). |
入库方式： OAI收割
来源：大连化学物理研究所
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