3P166 Free energy simulations for the conformational change of the αβ subunits in F_1-ATPase after the ATP hydrolysis(11. Molecular motor,Poster)

F1-ATPase is a protein complex to hydrolyze adenosine tri-phosphate (ATP).Within the complex, the part called β subunit carries the catalytic activity.In this study, we focus on the ATP binding of the β subunit and treat the β subunit isolated in solvent water.To separately treat the water and ATP effects on the binding, we conceptually decompose the binding process into two steps.The first step is the conformational change of the β subunit from the open to closed states.The second is the ATP binding to the closed state.The effect of water is taken into account at all-atom level using the molecular dynamics simulation coupled with the method of energy representation.We will show that the solvent water promotes the first step and inhibits the second.