The hypothesis was supported by figures that chart the sequence of β2AR – Gs complex. In Figure 2, the sequential nature of β2AR – Gs complex is evident. Particles from earliest time point (5s) constitute the predominate components of the initial intermediates (open AHD). Over time, contributions from later points (10s and 17s) increasingly dominate, correspondingly to the closed AHD state. Figure 3 makes clear that AHD closure alone does not cause major changes within the RHD. Instead, the presence of nucleotide is required to drive the extension of the α1 helix. Figure 4, in turn, supports the idea of functional dissociation. Finally, figure 5 brings the findings together, laying out how each structure shift plays out in sequence as GTP primes the G protein for action.