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This C&SP will focus on studying mechanisms of function of the complex biomolecular assembly of CaMKII and its dynamics. We recently showed that the human alpha isoform, CaMKIIalpha, literally acts as a device for propagating the activation by calcium signaling. This is achieved through subunit exchanges between activated CaMKII and holoenzyme assemblies that have not been activated. The spread of activation through these exchanges now suggests that activation can be maintained long after the disappearance of the initial signal. This is remarkable because it reveals a possible mechanism by which CaMKII assists in the induction of long-term memory in the brain. It is clear that the phosphorylation of the calmodulin-recognition element triggers the exchange. But in addition to localized interactions, there is something unique about the overall architecture of CaMKII so that it accommodates different oligomerization states. Starting from early crystal structures and EM images, we have seen that the holoenzyme could assume both dodecameric and tetradecameric forms. Our new observations now show that they coexist. An intriguing observation was: why does the vertical dimer dissociate, rather than a single subunit, or a horizontal dimer? ANM results unambiguously show that the dodecamer structure indeed favors the vertical dimers to be released. The type of analysis performed by ProDy can open the way to a better understanding of CaMKII dynamics. Additionally, coevolution analysis may give us additional information on interfacial interactions that modulate subunit exchange. These studies will help further understanding the dynamics and interactions of CaMKII. 2b1af7f3a8