Extended Data Fig. 3: Design of conformationally switchable rings that retain their oligomeric size upon effector binding.
From: De novo design of allosterically switchable protein assemblies
a. Schematic of double-hinge design, where peptide binding drives change in conformation, without altering oligomeric state. b. Double-hinge design pipeline with computational steps shown as a flowchart. c. Design models of sr508 in the X-state (pink, left) and Y-state (blue, right). d. SEC on 8 soluble double-hinge designs, where 3 μM GFP-tagged peptide was added to 3 μM protein. e. SEC on mixtures of sr508 (at 2 μM) and variable concentrations of GFP-tagged peptide. Color coding for different concentrations is shown on the top right. f. MP on sr503 in the presence (top) and absence ttom) of peptide, providing an example of a putatively non-cooperative design.
