A recent study based on molecular simulations and compliance constants describes molecular recognition as a phenomenon of organisation. Even for small molecules like carbohydrates, the recognition process can not be predicted or designed even assuming that each individual hydrogen bond's strength is exactly known. However, as Mobley et al. concluded, the accurate prediction of the molecular recognition events needs to go beyond the static snapshot of a single frame between the guest and the host. Entropies are key contributors to binding thermodynamics and need to be accounted for in order to predict more accurately the recognition process. Entropies are rarely observable in single bound structures (static snapshot). In proteins, highly-specific recognition can be achieved by evolutionary fine-tuning of chemical interactions, conformational changes, and entropy contributions.