Driven by increasing interests in sequencing proteins, several single molecule methods (such as the measurement of electron tunneling currents through each amino acid) have been recently proposed and demonstrated in experiment. While promising, they are still in early stages and challenges such as the lack of protein stretching and large thermal fluctuations of amino acids remain to be solved. Here, we show that a patterned two dimensional (2D) in-plane heterostructure comprising both graphene and hexagonal boron nitride (hBN) domains can be utilized to stretch the intrinsically disordered A β 42 protein because of the chemical potential difference between the graphene and hBN surfaces. Additionally, thanks to the physisorption of the flexible A β 42 protein on the 2D surface, thermal fluctuations of amino acids are substantially reduced. Therefore, this stretched protein conformation with amino acids adsorbed on the 2D surface may facilitate pr...

中文翻译：

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在图案化的二维纳米片上大力拉伸蛋白质

在人们对蛋白质测序的兴趣日益增长的驱动下，最近提出了几种单分子方法（例如测量通过每个氨基酸的电子隧穿电流），并在实验中得到了证明。尽管前景广阔，但它们仍处于早期阶段，诸如蛋白质缺乏拉伸和氨基酸的较大热波动等挑战仍待解决。在这里，我们表明，由于石墨烯和hBN之间的化学势差，包含石墨烯和六方氮化硼（hBN）域的二维二维（2D）平面内异质结构可用于拉伸内在无序的Aβ42蛋白。表面。另外，由于柔性Aβ42蛋白在2D表面上的物理吸附，大大减少了氨基酸的热波动。