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...
Главные авторы: | Martin, J, Ishmukhametov, R, Hornung, T, Ahmad, Z, Frasch, W |
---|---|
Формат: | Journal article |
Язык: | English |
Опубликовано: |
National Academy of Sciences
2014
|
Схожие документы
-
Determination of torque generation from the power stroke of Escherichia coli F1-ATPase
по: Hornung, T, и др.
Опубликовано: (2008) -
Elastic coupling power stroke mechanism of the F1-ATPase molecular motor
по: Martin, JL, и др.
Опубликовано: (2018) -
Abundance of Escherichia coli F1-ATPase molecules observed to rotate via single-molecule microscopy with gold nanorod probes.
по: York, J, и др.
Опубликовано: (2007) -
Abundance of Escherichia coli F1-ATPase molecules observed to rotate via single-molecule microscopy with gold nanorod probes
по: York, J, и др.
Опубликовано: (2007) -
Single molecule measurements of F1-ATPase reveal an interdependence between the power stroke and the dwell duration
по: Spetzler, D, и др.
Опубликовано: (2009)