Extended Data Fig. 3: SDS-PAGE analysis of in-solution treatment of autonomously compiled mCherry and mCerulean pendants.
From: Boolean logic-gated protein presentation through autonomously compiled molecular topology
a-c, Changes in topology and/or molecular weight in response to a specific set of inputs leads to changes in protein electrophoretic mobility, which can be analyzed through gel densitometry. Results are shown for species (a) mCherry-S, (b) mCerulean-T, and (c) mCerulean-S∧T. Plot titles correspond to the protein tether identity; the y-axis represents extent of cleavage as measured through migration on an SDS-PAGE with gel densitometry analysis; the x-axis indicates treatment conditions, wherein N indicates no treatment, A indicates eSrtA(2A9), S indicates eSrtA(4S9), and T indicates TEV. Error bars correspond to ±1 standard deviation about the mean with propagated uncertainties for n = 3 experimental replicates.
