The concept of spatial entropic redistribution extends our thinking of the contributors to the free energy of binding to the rest of the scaffold. This strategic transfer of entropy is likely a fundamental aspect of dynamic allostery, where proteins distribute their inherent disorder in a controlled manner to facilitate allosteric regulation. There are multiple mechanisms that nature can harness to optimize the entropic contribution from distal regions. These include 'entropic reservoirs', such as intrinsically disordered regions (IDRs) and local unfolding, and subtle conformational changes to well packed regions poised to increase side chain dynamics. This mechanistic diversity emphasizes how the optimization of free energy can come from unexpected places and calls attention to the opportunity for considering entropy to predictably tune binding affinity.