Donut-Shaped Fingerprint In Homologous Polypeptide Relationships-A Topological Feature Related To Pathogenic Structural Changes In Conformational Disease

doi:10.1016/j.jtbi.2009.02.009

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	Donut-Shaped Fingerprint In Homologous Polypeptide Relationships-A Topological Feature Related To Pathogenic Structural Changes In Conformational Disease
	Liu X(刘鑫); Zhao YP(赵亚溥); Zhao YP
发表期刊	Journal of Theoretical Biology
	2009
卷号	258 期号:2 页码:294-301
ISSN	0022-5193
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.
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
DOI	10.1016/j.jtbi.2009.02.009
收录类别	SCI
语种	英语
WOS记录号	WOS:000265801600014
关键词[WOS]	PREDICTING SIGNAL PEPTIDES ; STATE ENZYME-KINETICS ; PROTEIN-STRUCTURE ; GRAPHIC RULES ; CODON USAGE ; RATE LAWS ; EVOLUTION ; STEADY ; MODEL ; PRION
WOS研究方向	Life Sciences & Biomedicine - Other Topics ; Mathematical & Computational Biology
WOS类目	Biology ; Mathematical & Computational Biology
引用统计	被引频次：8[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://dspace.imech.ac.cn/handle/311007/26590
专题	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.

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