Molecular dynamics simulations provide increasingly accurate methods for characterizing biomolecular dynamics. However such simulations typically explore dynamics on the ps to ns timescale, while most processes of interest tend to occur on the ms to s timescale. As such there is a need enhanced for sampling methods to overcome this timescale issue. We propose a novel enhanced sampling method in which the dihedral and/or non-bonded potential energy terms are gently biased, such that the system is driven towards lower or higher energy conformations. Preliminary results show particular promise in the area of protein folding and small molecule dissociation. Several small proteins including an alpha helix, hairpin beta sheet, and TRP-CAGE motifs have been folded from extended conformations to within 1 A of their crystal structures with no previous knowledge of said crystal structures. Furthermore, the technique was found to drive dissociation of the avidin-biotin drug complex in under 1 ns. It is anticipated that this method can be extended to all flexible polymers such as DNA, RNA, and proteins. It is also anticipated to increase viability of small molecule binding simulations, allowing for locally enhanced sampling of association/dissociation events.