纳米片
纳米材料
亨廷顿蛋白
生物物理学
球状蛋白
两亲性
内在无序蛋白质
材料科学
折叠(DSP实现)
蛋白质折叠
纳米技术
分子动力学
石墨烯
蛋白质结构
结晶学
化学
生物化学
生物
计算化学
突变体
复合材料
共聚物
工程类
电气工程
聚合物
基因
作者
Leili Zhang,Mei Feng,Ruhong Zhou,Binquan Luan
出处
期刊:Nanotechnology
[IOP Publishing]
日期:2017-06-26
卷期号:28 (35): 354001-354001
被引量:12
标识
DOI:10.1088/1361-6528/aa7ba5
摘要
A globular protein's folded structure in its physiological environment is largely determined by its amino acid sequence. Recently, newly discovered transformer proteins as well as intrinsically disordered proteins may adopt the folding-upon-binding mechanism where their secondary structures are highly dependent on their binding partners. Due to the various applications of nanomaterials in biological sensors and potential wearable devices, it is important to discover possible conformational changes of proteins on nanomaterials. Here, through molecular dynamics simulations, we show that the first 17 residues of the huntingtin protein (HTT-N17) exhibit appreciable differences during its folding on 2D-nanomaterials, such as graphene and MoS2 nanosheets. Namely, the protein is disordered on the graphene surface but is helical on the MoS2 surface. Despite that the amphiphilic environment at the nanosheet-water interface promotes the folding of the amphipathic proteins (such as HTT-N17), competitions between protein-nanosheet and intra-protein interactions yield very different protein conformations. Therefore, as engineered binding partners, nanomaterials might significantly affect the structures of adsorbed proteins.
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