Pages that link to "Q34048262"
Jump to navigation
Jump to search
The following pages link to Rapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sites (Q34048262):
Displaying 10 items.
- Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides (Q27653878) (← links)
- Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase (Q27939194) (← links)
- Temperature dependence of the rotation and hydrolysis activities of F1-ATPase (Q33326233) (← links)
- Ecto-F₁-ATPase: a moonlighting protein complex and an unexpected apoA-I receptor (Q34428768) (← links)
- Studies of nucleotide binding to the catalytic sites of Escherichia coli betaY331W-F1-ATPase using fluorescence quenching (Q35721341) (← links)
- The structure and function of mitochondrial F1F0-ATP synthases (Q37188087) (← links)
- FoF1-ATPase, rotary motor and biosensor (Q37785787) (← links)
- Chemo-mechanical coupling in F(1)-ATPase revealed by catalytic site occupancy during catalysis (Q39887594) (← links)
- Engineering a light-controlled F1 ATPase using structure-based protein design (Q42379356) (← links)
- ATP hydrolysis-driven H(+) translocation is stimulated by sulfate, a strong inhibitor of mitochondrial ATP synthesis (Q46322234) (← links)