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题名: COMPARING FOLDING MECHANISMS OF DIFFERENT PRION PROTEINS BY G(o)over-bar MODEL
作者: Wu, Xue1, 2, 3;  Fu, Ting1, 2, 3;  Xiu, Zhi-Long1;  Yin, Liu4;  Wang, Jin-Guang5;  Li, Guo-Hui2
关键词: Prion protein ;  fold ;  Go model ;  cooperativity ;  stability
刊名: JOURNAL OF THEORETICAL & COMPUTATIONAL CHEMISTRY
发表日期: 2013-12-01
DOI: 10.1142/S0219633613410046
卷: 12, 期:8
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Physical Sciences
类目[WOS]: Chemistry, Multidisciplinary
研究领域[WOS]: Chemistry
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.
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
语种: 英语
WOS记录号: WOS:000328359500004
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/137653
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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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

Recommended Citation:
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).
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