Biophysical Journal 85 3

Cover:Molecular dynamics simulations provide information on the conformational dynamics of F1-ATPase (A–C). For different substrate occupancies, different conformations of the β-subunit are obtained from the simulations and compared to the crystal structures (D, from Gibbons et al., 2000). The empty, initially open β-subunit closes spontaneously (A and B), whereas the closed β-subunit displays a sideward pivoting motion (C) when the substrate is removed. The arrows indicate axes of domain motions. See the article by Böckmann and Grubmüller on p. 1482.