生物信息学2012，Vol.10Issue(3)：158-162,5.DOI:10.3969/j.issn.1672-5565.2012.03.03
Val55点突变对鸡胱抑素I66Q结构稳定性影响的分子动力学研究
Molecular Dynamics Simulation for the Effect of Val55 Mutations on the Structural Stability of Chicken Cystatin I66Q
摘要
Abstract
Residue Val55 plays a significant role in the hinge loop of the chicken cystatin ( cC) . In this study,mo-lecular dynamics simulations were preformed to investigate effect of Val55 mutation on the structural stability of a typical amyloidogenic cC mutant I66Q,and explored the possible mechanism. It was found that both V55N and V55D could enhance the structural stability of cC I66Q,especially in the case of V55N. Future research indicates that there were more hydrogen bonds related with position 55 in V55N and V55D mutants. This led to increasing the stability of Loopl and β2 - β3,which stabilized the a - helix and hydrophobic core of cC I66Q. These listed factors might inhibit the process of domain swapping of cC I66Q.关键词
胱抑素/淀粉样聚集/分子动力学模拟/结构域交换Key words
cystatin/amyloid/molecular dynamics simulation/domain swapping分类
农业科技引用本文复制引用
张梦媛,徐利楠,沈曼莉,何剑为,宋有涛..Val55点突变对鸡胱抑素I66Q结构稳定性影响的分子动力学研究[J].生物信息学,2012,10(3):158-162,5.基金项目
国家自然科学基金(30970152)和辽宁省教育厅优秀人才项目(2009R26)资助. （30970152）
