Donut-Shaped Fingerprint In Homologous Polypeptide Relationships-A Topological Feature Related To Pathogenic Structural Changes In Conformational Disease
文献类型：期刊论文
| 作者 | Liu X(刘鑫) ; Zhao YP(赵亚溥); Zhao YP
|
| 刊名 | Journal of Theoretical Biology
 |
| 出版日期 | 2009 |
| 卷号 | 258期号:2页码:294-301 |
| 通讯作者邮箱 | liuxin@lnm.imech.ac.cn; yzhao@imech.ac.cn |
| 关键词 | Homologous Relationship Polypeptide Prion Protein Conformational Disease Predicting Signal Peptides State Enzyme-Kinetics Protein-Structure Graphic Rules Codon Usage Rate Laws Evolution Steady Model Prion |
| ISSN号 | 0022-5193 |
| 通讯作者 | Zhao YP |
| 中文摘要 | Features of homologous relationship of proteins can provide us a general picture of protein universe, assist protein design and analysis, and further our comprehension of the evolution of organisms. Here we carried Out a Study of the evolution Of protein molecules by investigating homologous relationships among residue segments. The motive was to identify detailed topological features of homologous relationships for short residue segments in the whole protein universe. Based on the data of a large number of non-redundant Proteins, the universe of non-membrane polypeptide was analyzed by considering both residue mutations and structural conservation. By connecting homologous segments with edges, we obtained a homologous relationship network of the whole universe of short residue segments, which we named the graph of polypeptide relationships (GPR). Since the network is extremely complicated for topological transitions, to obtain an in-depth understanding, only subgraphs composed of vital nodes of the GPR were analyzed. Such analysis of vital subgraphs of the GPR revealed a donut-shaped fingerprint. Utilization of this topological feature revealed the switch sites (where the beginning of exposure Of previously hidden "hot spots" of fibril-forming happens, in consequence a further opportunity for protein aggregation is Provided; 188-202) of the conformational conversion of the normal alpha-helix-rich prion protein PrPC to the beta-sheet-rich PrPSc that is thought to be responsible for a group of fatal neurodegenerative diseases, transmissible spongiform encephalopathies. Efforts in analyzing other proteins related to various conformational diseases are also introduced. (C) 2009 Elsevier Ltd. All rights reserved. |
| 类目[WOS] | Biology ; Mathematical & Computational Biology |
| 研究领域[WOS] | Life Sciences & Biomedicine - Other Topics ; Mathematical & Computational Biology |
| 关键词[WOS] | PREDICTING SIGNAL PEPTIDES ; STATE ENZYME-KINETICS ; PROTEIN-STRUCTURE ; GRAPHIC RULES ; CODON USAGE ; RATE LAWS ; EVOLUTION ; STEADY ; MODEL ; PRION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000265801600014 |
| 公开日期 | 2009-08-03 ; 2009-10-09 |
| 源URL | [http://dspace.imech.ac.cn/handle/311007/26590]  |
| 专题 | 力学研究所_非线性力学国家重点实验室 |
| 通讯作者 | Zhao YP |
| 推荐引用方式 GB/T 7714 | Liu X,Zhao YP,Zhao YP. Donut-Shaped Fingerprint In Homologous Polypeptide Relationships-A Topological Feature Related To Pathogenic Structural Changes In Conformational Disease[J]. Journal of Theoretical Biology,2009,258(2):294-301. |
| APA | 刘鑫,赵亚溥,&Zhao YP.(2009).Donut-Shaped Fingerprint In Homologous Polypeptide Relationships-A Topological Feature Related To Pathogenic Structural Changes In Conformational Disease.Journal of Theoretical Biology,258(2),294-301. |
| MLA | 刘鑫,et al."Donut-Shaped Fingerprint In Homologous Polypeptide Relationships-A Topological Feature Related To Pathogenic Structural Changes In Conformational Disease".Journal of Theoretical Biology 258.2(2009):294-301. |
入库方式： OAI收割
来源：力学研究所
浏览0
下载0
收藏0
其他版本
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。