While concerted structural changes are clearly important for allostery, there is mounting evidence that conformational disorder has an important role to play, and can even lead to allosteric communication in the absence of concerted structural ,transitions . The importance of allostery without conformational change first appeared in a model where ligand binding perturbs the entropy of a distant site rather than its preferred structure . In recent years the role of conformational entropy in allosteric communication has been increasingly acknowledged. The importance of conformational entropy was first described theoretically in 1984 by Cooper and Dryden . Since then experimental evidence for this "dynamical allostery" has grown. Particularly, NMR data demonstrated two sites on a transcription factor were coupled with no discernible structural changes . Furthermore, intrinsically disordered regions can also play a role in allosteric coupling, as normally ordered regions of a protein may transition locally into higher-entropy excited states that rapidly hop between multiple thermodynamic minima. This flattening of the effective free energy surface for a set of residues distinguishes dynamic allostery from the previously discussed mechanism of concerted structural To infer allostery and coupling between distal residues, per-residue structural features (i.e. dihedrals) can be extracted (right column) and converted into structural states (such as rotamers) and dynamical states (representing low or high entropic behaviors). From these states, mutual information can be used to infer the degree of structural and dynamical allostery within the system. Message Passing algorithms can then be used to infer an allosteric network between protein communities (lower right). changes. More recently, it has become apparent that to understand a protein's allosteric network, it is important to observe both concerted structural changes and altered conformational entropy . The ability to construct allosteric networks, by measuring both structure and disorder, has the potential to explain the mechanism of coupling in many complex biological process and may present opportunities to identify promising druggable pockets and the role they play in modulating protein function.