The affinity purification and characterization of ATP synthase complexes from mitochondria

@inproceedings{Runswick2013TheAP,
  title={The affinity purification and characterization of ATP synthase complexes from mitochondria},
  author={Michael J. Runswick and John V. Bason and Martin G. Montgomery and Graham C. Robinson and Ian M. Fearnley and John E Walker},
  booktitle={Open biology},
  year={2013}
}
The mitochondrial F₁-ATPase inhibitor protein, IF₁, inhibits the hydrolytic, but not the synthetic activity of the F-ATP synthase, and requires the hydrolysis of ATP to form the inhibited complex. In this complex, the α-helical inhibitory region of the bound IF₁ occupies a deep cleft in one of the three catalytic interfaces of the enzyme. Its N-terminal region penetrates into the central aqueous cavity of the enzyme and interacts with the γ-subunit in the enzyme's rotor. The intricacy of… CONTINUE READING
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