Fig. 2. Characterization of designed small proteins using a protease-based high throughput screen on the yeast surface and biochemical analysis of individually expressed proteins.

a Cartoon scheme of yeast surface display experiment. Unfolded proteins are cleaved and, thereby, will not be fluorescently labeled. b FITC fluorescence after incubation of yeast cells displaying the designed proteins as a pool with increasing concentration of trypsin; cells were labeled with a c-Myc antibody conjugated to FITC. c Trypsin and chymotrypsin stability of previously evaluated proteins with known stability scores were included in the pool of the query proteins as a “stability score ladder” to help adjust for protease activities. d The number of designs from each fold with indicated stability score or higher was used to compute e the “success rate” of each designed topology for a given stability score bin. Source data is provided as Source Data File.