DICP OpenIR
COMPARING FOLDING MECHANISMS OF DIFFERENT PRION PROTEINS BY G(o)over-bar MODEL
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
2013-12-01
DOI10.1142/S0219633613410046
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
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
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.
语种英语
WOS记录号WOS:000328359500004
引用统计
文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/137653
专题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).
条目包含的文件
条目无相关文件。
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Wu, Xue]的文章
[Fu, Ting]的文章
[Xiu, Zhi-Long]的文章
百度学术
百度学术中相似的文章
[Wu, Xue]的文章
[Fu, Ting]的文章
[Xiu, Zhi-Long]的文章
必应学术
必应学术中相似的文章
[Wu, Xue]的文章
[Fu, Ting]的文章
[Xiu, Zhi-Long]的文章
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。