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Showing 1 to 4 of 4 for “"nanomotor"”.

  1. Modeling of the dynamics of autonomous catalytic nanomotors using the method of regularized stokeslets

    Catalytic nanomotors move autonomously by deriving energy directly from their environment, mimicking biological nanomotors that perform a wide range of complex functions at the cellular level and drive vital functions such as active transport, muscle contraction, cell mobility, and other movement. …

    uiuc Repository record for Modeling of the dynamics of autonomous catalytic nanomotors using the method of regularized stokeslets (opens in a new tab)

  2. Structure and Function Study of Phi29 DNA packaging motor

    <p>A powerful nanomotor is employed by the tailed dsDNA virus to package the genome into a preformed protein shell during the process of replication. The bacteriophage phi29 is an excellent model for investigating the viral DNA packaging mechanism. The phi29 DNA packaging motor is composed of three …

    ohiolink Repository record for Structure and Function Study of Phi29 DNA packaging motor (opens in a new tab)

  3. Inhibition of <em>Escherichia coli</em> ATP Synthase by Polyphenols and Their Derivatives.

    <p>We have studied the inhibitory effect of natural and structurally modified polyphenols on <em>Escherichia coli</em> ATP synthase to test (I) if the beneficial dietary effects of polyphenols are related to their inhibitory actions on ATP synthase, (II) if inhibitory effects of polyphenolic …

    etsu Repository record for Inhibition of <em>Escherichia coli</em> ATP Synthase by Polyphenols and Their Derivatives. (opens in a new tab)

  4. Molecular Modulation of a-Subunit VISIT-DG Sequence Residue Asp-350 in the Catalytic sites of <em>Escherichia coli</em> ATP Synthase.

    <p>ATP Synthase is the fundamental means of cellular energy production in animals, plants, and almost all microorganisms. In order to understand the mechanism of ATP catalysis, critical amino acid residues involved in Pi binding have to be identified. The αVISIT-DG sequence at the interface of α/β …

    etsu Repository record for Molecular Modulation of a-Subunit VISIT-DG Sequence Residue Asp-350 in the Catalytic sites of <em>Escherichia coli</em> ATP Synthase. (opens in a new tab)