Molecular dynamics study on the stability of wild-type and the R220K mutant of human prion protein

被引：8

作者：

Chen, Xin ^{[1
]}

Zhu, Shuyan ^{[1
]}

Wang, Shoubin ^{[1
]}

Yang, Dagang ^{[1
]}

Zhang, Jinglai ^{[1
]}

机构：

[1] Henan Univ, Inst Environm & Analyt Sci, Coll Chem & Chem Engn, Kaifeng 475001, Henan, Peoples R China

来源：

MOLECULAR SIMULATION | 2014年 / 40卷 / 06期

基金：

中国国家自然科学基金;

关键词：

stability; mutant; molecular dynamics simulation; hydrodynamics; human prion protein; GLYCOPROTEIN-IB; BETA-SWITCH; LOW PH; TEMPERATURE; SIMULATION; DISEASES; TRANSITION; VARIANTS; MUTATION; BIOLOGY;

D O I：

10.1080/08927022.2013.824572

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Prion diseases are invariably fatal and highly infectious neurodegenerative diseases related to the structure transition of -helix into -sheet. In order to gain more direct insight into the molecular basis of the disease, the stability of the wild-type human prion protein (hPrPc) and the R220K mutant (m-hPrPc) was studied by molecular dynamics (MD) and flow MD simulation. Both the thermodynamic stability and the mechanical properties of hPrPc were investigated in this work. It was found that -sheet was more readily to be unfolded in m-hPrPc. In the case of hPrPc, less content of helix was preserved after water turbulence. The H-bond network formed by the mutation-related residue 220 was found to play a key role in the stability of hPrPc.

引用

页码：504 / 513

页数：10

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