Some proteins are conformational switches, able to transition between relatively different conformations. To understand what drives them requires computing the free-energy difference ΔGAB between their stable states, A and B. Molecular dynamics (MD) simulations alone are often slow because they require a reaction coordinate and must sample many transitions in between. Here, we show that modeling employing limited data (MELD) x MD on known endstates A and B is accurate and efficient because it does not require passing over barriers or knowing reaction coordinates. We validate this method on two problems: (1) it gives correct relative populations of α and β conformers for small designed chameleon sequences of protein G; and (2) it correctly predicts the conformations of the C-terminal domain (CTD) of RfaH. Free-energy methods like MELD x MD can often resolve structures that confuse machine-learning (ML) methods.