The idea that a protein's conformational landscape can impact its allosteric behavior leads one to speculate if all proteins have some degree of allosteric coupling . Indeed, the ubiquity of allostery has been acknowledged in studies of natural and directed evolution [109? ], where mutations distant from the active site can impact measured properties. Given the potentially universal nature of allostery, it is worth speculating if mutations and ligands work by tapping into existing allosteric networks to modulate the distributions of a protein's of structures and dynamics . Thus, understanding allosteric coupling in proteins could present new opportunities for modulating biological processes, designing therapeutics, or even designing new proteins.