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Small mechanical forces play important functional roles in many crucialcellular processes, including in the dynamical behavior of the cytoskeleton andin the regulation of osmotic pressure through membrane-bound proteins.Molecular simulations offer the promise of being able to design the behavior ofproteins that sense and respond to these forces. However, it is difficult topredict and identify the effect of the relevant piconewton (pN) scale forcesdue to their small magnitude. Previously, we introduced the Infinite SwitchSimulated Tempering in Force (FISST) method which allows one to estimate theeffect of a range of applied forces from a single molecular dynamicssimulation, and also demonstrated that FISST additionally accelerates samplingof a molecule's conformational landscape. For some problems, we find that thisacceleration is not sufficient to capture all relevant conformationalfluctuations, and hence here we demonstrate that FISST can be combined witheither temperature replica exchange or solute tempering approaches to produce ahybrid method that enables more robust prediction of the effect of small forceson molecular systems.

Improved prediction of molecular response to pulling by combining force tempering with replica exchange methods