English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

F1-ATPase is the soluble portion of the membrane-embedded enzyme FoF1-ATPsynthase that catalyzes the production of adenosine triphosphate in eukaryoticand eubacterial cells. In reverse, the F1 part can also hydrolyze ATP quicklyat three catalytic binding sites. Therefore, catalysis of 'non-productive' ATPhydrolysis by F1 (or FoF1) must be minimized in the cell. In bacteria, theepsilon subunit is thought to control and block ATP hydrolysis by mechanicallyinserting its C-terminus into the rotary motor region of F1. We investigatethis proposed mechanism by labeling F1 specifically with two fluorophores tomonitor the C-terminus of the epsilon subunit by F\"orster resonance energytransfer. Single F1 molecules are trapped in solution by an Anti-Brownianelectrokinetic trap which keeps the FRET-labeled F1 in place for extendedobservation times of several hundreds of milliseconds, limited byphotobleaching. FRET changes in single F1 and FRET histograms for differentbiochemical conditions are compared to evaluate the proposed regulatorymechanism.

The regulatory switch of F1-ATPase studied by single-molecule FRET in the ABEL Trap