Determining the occurrence of motifs yields profound insight for many biological systems, like metabolic, protein-protein interaction, and protein structure networks. Meaningful spatial protein-structure motifs include enzyme active sites and ligand-binding sites which are essential for function, shape, and performance of an enzyme. Analyzing their dynamics over time leads to a better understanding of underlying properties and processes. In this work, we present StreaM, a stream-based algorithm for counting undirected 4-vertex motifs in dynamic graphs. We evaluate StreaM against the four predominant approaches from the current state of the art on generated and real-world datasets, a simulation of a highly dynamic enzyme. For this case, we show that StreaM is capable to capture essential molecular protein dynamics and thereby provides a powerful method for evaluating large molecular dynamics trajectories. Compared to related work, our approach achieves speedups of up to 2,300 times on real-world datasets.
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