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The Rel proteins of the NF‐κB complex comprise one of the most investigated transcription factor families, forming a variety of hetero‐ or homodimers. Nevertheless, very little is known about the fundamental kinetics of NF‐κB complex assembly, or the inter‐conversion potential of dimerised Rel subunits. Here, we examined an unexplored aspect of NF‐κB dynamics, focusing on the dissociation and reassociation...