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Dynamic behavior of a rotary nanomotor in argon environments.

ABSTRACT: When argon is used as a protecting gas in the fabrication or working environment of a nanodevice, absorption of some argon atoms onto the surface of the device lead to different responses. In this work, the rotation of the rotor in a carbon nanotube (CNT)-based rotary nanomotor in argon environment is investigated. In the rotary nanomotor, two outer CNTs act as the stator and are used to constrain the inner CNT (i.e., the rotor). The rotor is driven to rotate by the stator due to their collision during thermal vibration of their atoms. A stable rotational frequency (SRF) of the rotor occurs when the rotor reaches a dynamic equilibrium state. The value of the SRF decreases exponentially with an increase in the initial argon density. At dynamic equilibrium date, some of the argon atoms rotate synchronously with the rotor when they are absorbed onto either internal or external surface of the rotor. The interaction between the rest of the argon atoms and the rotor is stronger at higher densities of argon, resulting in lower values of the SRF. These principles provide insight for future experimentation and fabrication of such rotary nanomotor.

SUBMITTER: Cai K

PROVIDER: S-EPMC5823920 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

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Dynamic behavior of a rotary nanomotor in argon environments.

Cai Kun K Shi Jiao J Yu Jingzhou J Qin Qing H QH

Scientific reports 20180222 1

When argon is used as a protecting gas in the fabrication or working environment of a nanodevice, absorption of some argon atoms onto the surface of the device lead to different responses. In this work, the rotation of the rotor in a carbon nanotube (CNT)-based rotary nanomotor in argon environment is investigated. In the rotary nanomotor, two outer CNTs act as the stator and are used to constrain the inner CNT (i.e., the rotor). The rotor is driven to rotate by the stator due to their collision ...[more]

PMID: 29472545

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Project description:The F(1)F(0)-adenosine triphosphate (ATP) synthase rotational motor synthesizes most of the ATP required for living from adenosine diphosphate, Pi, and a proton electrochemical gradient across energy-transducing membranes of bacteria, chloroplasts, and mitochondria. However, as a reversible nanomotor, it also hydrolyzes ATP during de-energized conditions in all energy-transducing systems. Thus, different subunits and mechanisms have emerged in nature to control the intrinsic rotation of the enzyme to favor the ATP synthase activity over its opposite and commonly wasteful ATPase turnover. Recent advances in the structural analysis of the bacterial and mitochondrial ATP synthases are summarized to review the distribution and mechanism of the subunits that are part of the central rotor and regulate its gyration. In eubacteria, the epsilon subunit works as a ratchet to favor the rotation of the central stalk in the ATP synthase direction by extending and contracting two alpha-helixes of its C-terminal side and also by binding ATP with low affinity in thermophilic bacteria. On the other hand, in bovine heart mitochondria, the so-called inhibitor protein (IF(1)) interferes with the intrinsic rotational mechanism of the central gamma subunit and with the opening and closing of the catalytic beta-subunits to inhibit its ATPase activity. Besides its inhibitory role, the IF(1) protein also promotes the dimerization of the bovine and rat mitochondrial enzymes, albeit it is not essential for dimerization of the yeast F(1)F(0) mitochondrial complex. High-resolution electron microscopy of the dimeric enzyme in its bovine and yeast forms shows a conical shape that is compatible with the role of the ATP synthase dimer in the formation of tubular the cristae membrane of mitochondria after further oligomerization. Dimerization of the mitochondrial ATP synthase diminishes the rotational drag of the central rotor that would decrease the coupling efficiency between rotation of the central stalk and ATP synthesis taking place at the F(1) portion. In addition, F(1)F(0) dimerization and its further oligomerization also increase the stability of the enzyme to natural or experimentally induced destabilizing conditions.

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Dynamic behavior of a rotary nanomotor in argon environments.

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Dynamic behavior of a rotary nanomotor in argon environments.

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