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Structure-dependent electrical conductivity of protein: its differences between alpha-domain and beta-domain structures

机译：蛋白质的结构依赖性电导率：其α结构域和β结构域结构之间的差异

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摘要

Electron transports in the alpha-domain and beta-domain of proteins have been comprehensively investigated. The structure-dependent electron transport of proteins has been experimentally measured and theoretically simulated, and both the theoretical and experimental results demonstrate significant differences in electrical conductivity between the alpha-domain and beta-domain. By controlling the feedback system of the scanning tunneling microscope (STM), the conductance of a single alpha-domain protein hemoglobin (Hgb) and a beta-domain protein superoxide dismutase enzyme (SOD) were measured, respectively. The current signal of Hgb is obviously stronger, indicating that the alpha-domain is more conductive. To confirm our finding, molecular orbitals of both the beta-domain in SOD and alpha-domain in Hgb have been analyzed based on first-principles calculations. As expected, tunneling transport and hopping in the alpha-domain are both more efficient, indicating that it is easier for electrons to transport through the beta-domain, which are in great agreement with our experimental data. In order to explain our results, molecular structures of alpha- and beta-domains have been carefully analyzed and show that the explanation should lie in the differences in packing mode between the alpha-domain and beta-domain. This research should be very important to application prospects in molecular electronics.
机译：已经全面研究了蛋白质的α-结构域和β-结构域中的电子传输。蛋白质的结构依赖性电子传输已通过实验测量和理论模拟，并且理论和实验结果均表明，α结构域和β结构域之间的电导率存在显着差异。通过控制扫描隧道显微镜（STM）的反馈系统，分别测量了单个α结构域蛋白血红蛋白（Hgb）和β结构域蛋白超氧化物歧化酶（SOD）的电导。 Hgb的电流信号明显更强，表明α域的导电性更高。为了证实我们的发现，已经根据第一性原理分析了SOD中的β域和Hgb中的α域的分子轨道。不出所料，在α域中的隧穿传输和跳跃都更有效，这表明电子更容易通过β域传输，这与我们的实验数据高度吻合。为了解释我们的结果，已经仔细分析了α-和β-结构域的分子结构，表明解释应该在于α-结构域和β-结构域之间堆积方式的差异。这项研究对于分子电子学中的应用前景应该是非常重要的。

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