Assembly in the translation milieu imposes evolutionary constraints on homomeric proteins

<b>Supplementary Video 1. Simulation</b> <b>of Tet@N with short linker. </b>For all movies the red segment is the Tet, and yellow is the YFP beta-barrel. Both cotranslational folding and misassembly take place once the Tet appear outside of the ribosome tunnels.<br> <b>Supplementary Video 2. Simulation</b> <b>of Tet@C with short linker. </b>There was no cotranslational assembly as the Tet of the leading ribosome leaves the ribosomal tunnel prior to the translation of the second ribosome, which allows it time to diffuse before the second Tet leaves the ribosome tunnel. <b> </b> <b>Supplementary Video 3. Simulation</b> <b>of Tet@N with long linker. </b>Cotranslational assembly takes place, but not misassembly. Similarly to movies S1-S2, the red segment is the Tet and the yellow is the YFP reporter-gene, the cyan segment is the long-linker. The less frequent misassembly events fit the observed <i>in vivo and in vitro</i> data. <b> </b>