Cells employ a variety of linear motors, such as myosin 1–3 , kinesin 4 and RNA polymerase
5 , which move along and exert force on a filamentous structure. But only one rotary motor …

ATP synthase can be thought of as a complex of two motors — the ATP-driven F 1 motor and
the proton-driven F o motor — that rotate in opposite directions. The mechanisms by which …

ATP synthase couples transmembrane proton transport, driven by the proton motive force (pmf),
to the synthesis of ATP from ADP and inorganic phosphate (P i ). In certain bacteria, the …

A single molecule of F 1 -ATPase, a portion of ATP synthase, is by itself a rotary motor in
which a central γ subunit rotates against a surrounding cylinder made of α 3 β 3 subunits. …

The enzyme F 1 -ATPase has been shown to be a rotary motor in which the central γ-subunit
rotates inside the cylinder made of α 3 β 3 subunits. At low ATP concentrations, the motor …

Active transport across the vacuolar components of the eukaryotic endomembrane system is
energized by a specific vacuolar H+-ATPase. The amino acid sequences of the 70- and 60-…

ATP, the main biological energy currency, is synthesized from ADP and inorganic phosphate
by ATP synthase in an energy-requiring reaction 1 , 2 , 3 . The F 1 portion of ATP synthase, …

Molecular chaperones assist protein folding by facilitating their "forward" folding and
preventing aggregation. However, once aggregates have formed, these chaperones cannot …

F 1 -ATPase is a rotary molecular motor that proceeds in 120 steps, each driven by ATP
hydrolysis. How the chemical reactions that occur in three catalytic sites are coupled to …

F 1 -ATPase is a rotary molecular motor in which unidirectional rotation of the central γ
subunit is powered by ATP hydrolysis in three catalytic sites arranged 120 apart around γ. To …