Anatomy of F1-ATPase powered rotation.
F1-ATPase, the catalytic complex of the ATP synthase, is a molecular motor that can consume ATP to drive rotation of the γ-subunit inside the ring of three αβ-subunit heterodimers in 120° power strokes. To elucidate the mechanism of ATPase-powered rotation, we determined the angular velocity as a fu...
Hoofdauteurs: | Martin, J, Ishmukhametov, R, Hornung, T, Ahmad, Z, Frasch, W |
---|---|
Formaat: | Journal article |
Taal: | English |
Gepubliceerd in: |
National Academy of Sciences
2014
|
Gelijkaardige items
-
Determination of torque generation from the power stroke of Escherichia coli F1-ATPase
door: Hornung, T, et al.
Gepubliceerd in: (2008) -
Elastic coupling power stroke mechanism of the F1-ATPase molecular motor
door: Martin, JL, et al.
Gepubliceerd in: (2018) -
Abundance of Escherichia coli F1-ATPase molecules observed to rotate via single-molecule microscopy with gold nanorod probes.
door: York, J, et al.
Gepubliceerd in: (2007) -
Abundance of Escherichia coli F1-ATPase molecules observed to rotate via single-molecule microscopy with gold nanorod probes
door: York, J, et al.
Gepubliceerd in: (2007) -
Single molecule measurements of F1-ATPase reveal an interdependence between the power stroke and the dwell duration
door: Spetzler, D, et al.
Gepubliceerd in: (2009)