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  1. Fast ATP-Dependent Subunit Rotation in Reconstituted F o F 1 -ATP Synthase Trapped in Solution

    This article has 2 authors:
    1. Thomas Heitkamp
    2. Michael Börsch
    This article has been curated by 1 group:
    • Curated by Biophysics Colab

      Endorsement statement (21 September 2021)

      The preprint by Heitkamp and Börsch describes visualization of the fast ATP-dependent subunit rotation in reconstituted FoF1-ATP synthase using single-molecule FRET techniques. Using a highly innovative method for trapping single molecules, the authors were able to see the static and dynamic disorder of enzymes in solution, not possible in previous studies. The work makes important contributions to both understanding the structural dynamics of FoF1-ATP synthase and the development of methodologies to study single-molecule dynamics of other proteins in solution.

      (This endorsement refers to version 5 of this preprint, which was peer reviewed by Biophysics Colab.)

    Reviewed by Biophysics Colab

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