Due to the challenges associated with the synthesis and especially the characterization of potential foldamer molecules, molecular dynamics (MD) simulations are a vital tool for searching broad chemical spaces and efficiently exploring folding properties such as stability and cooperativity. Moreover, MD simulations provide a direct atomic-level (or coarsegrained particle-level) view of secondary structures. Recent progress in enhanced sampling methods, statistical analysis techniques, sheer computing power, and the quality of both atomistic and coarse-grained force fields have paved the way for increasingly accurate simulations of molecular folding. Previous experimental and simulation efforts of foldamers have largely focused on biosimilar molecules resembling proteins, DNA, or RNA. Yet, biological foldamers represent only a miniscule fraction of chemical space, and their chemical sequences have been constrained by evolutionary pressure to perform specific biological functions in a specific biological environment. Without these constraints, carefully designed foldamers with non-natural backbones can have several advantages-for example, they can be more chemically resilient, especially with regard to resistance to hydrolysis, or exhibit superior mechanical and electrical properties not possible with a peptidic backbone.