Showing 821 - 840 results of 102,778 for search '(( 2 step decrease ) OR ( 5 ((((we decrease) OR (a decrease))) OR (nn decrease)) ))', query time: 1.50s Refine Results
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  6. 826

    Activation of mitoK<sub>ATP</sub> channels decreased the latency time of the transjunctional currents in slice. by Jiangping Wang (281901)

    Published 2013
    “…<p>(<b>A</b>) Currents in S<sub>cell</sub> induced by a pair of ±160 mV voltage steps and the transjunctional currents received by the R<sub>cell</sub>. …”
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  12. 832

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    Published 2009
    “…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
  13. 833

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    Published 2009
    “…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
  14. 834

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    Published 2009
    “…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
  15. 835

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    Published 2009
    “…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
  16. 836

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    Published 2009
    “…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
  17. 837

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    Published 2009
    “…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
  18. 838

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    Published 2009
    “…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
  19. 839

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    Published 2009
    “…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”
  20. 840

    Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, a... by Dhruva K. Chakravorty (1420549)

    Published 2009
    “…The carboxylate group of the Asp38 side chain, which serves as the proton acceptor and donor in the first and second steps, respectively, rotates significantly between the two proton transfer reactions. …”