Elastic energy storage in β-sheets with application to F1-ATPase

We present a methodology for obtaining the elastic properties of protein motifs. We combine the use of interpolated structures (IS), molecular dynamics (MD) and collective coordinates to deduce the elastic properties of the β-sheet in F1 ATPase. We find that about 3.5 kcal/mol (6 kBT at room temperature) of elastic energy is stored in the β-sheet as the β-subunit undergoes its hinge bending motion, in good agreement with the finite element model of Wang and Oster [Nature (1998) 396:279–282]. The technique should be useful for β-sheets in other proteins and aid in the construction of phenomenological models for molecular motors that are computationally prohibitive for MD alone.