Thread: NMR paper Structural analysis of ATP bound to the F(1)-ATPase beta-subunit monomer by solid-state NMR- insight into the hydrolysis mechanism in F(1)
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Default Structural analysis of ATP bound to the F(1)-ATPase beta-subunit monomer by solid-state NMR- insight into the hydrolysis mechanism in F(1)
Structural analysis of ATP bound to the F(1)-ATPase beta-subunit monomer by solid-state NMR- insight into the hydrolysis mechanism in F(1)

ATP-hydrolysis-associated conformational change of the ?-subunit during the rotation of F(1)-ATPase (F(1)) has been discussed using cryo-electron microscopy (cryo-EM). Since it is worthwhile to further investigate the conformation of ATP at the catalytic subunit through an alternative approach, the structure of ATP bound to the F(1)?-subunit monomer (?) was analyzed by solid-state NMR. The adenosine conformation of ATP-? was similar to that of ATP analog in F(1) crystal structures. ^(31)P...

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