Proteins are highly dynamic as they interact with hormones, ions, and other types of signaling molecules as well as other proteins. The motions that mediate these interactions comprise both large and small remodeling events, such as the shifting of domains to facilitate access to a catalytic site or the flipping of sidechain rotamers in an active site to accommodate a binding event. Classical molecular simulations have proven a valuable tool for understanding these motions, and in some cases, quantitatively predicting properties like binding affinity or the kinetics for structural transitions. Unfortunately, some of these motions are still difficult to model and predict even as advances in computing power make longer timescale motions more accessible. But in some cases, simulation timescales are still not long enough to capture the relevant motions, and such difficulties are often called "sampling problems". Some motions are expected to be slow. For example, allosteric remodeling, protein unfold-ing, and ligand binding can often take microseconds to seconds. In contrast, simple sidechain rotations are often faster in comparison but can still take anywhere from ps to several hundred ns, or even longer in the interior of proteins thus, they too can present sampling problems. Such motions are often simpler to detect and more tractable for sampling improvements than larger-scale rearrangements in biomolecules. As such, our particular focus here is on accelerating sidechain motions with our enhanced sampling methodology.