Fig. 9
From: Design of symmetric TIM barrel proteins from first principles
Additional experimental characterization of Symmetrin-1. a The Symmetrin-1 backbone model is shown in white. All aromatic residues are colored green. b The near-ultraviolet circular dichroism (CD) spectrum is shown, signifying immobilized aromatic residues. c Thermal unfolding and refolding assay, recorded at 222 nm from 10-75 °C. Unfolding data (heating schedule) is shown in red. Refolding data (cooling schedule) is shown in blue. d Chemical denaturation recorded at 222 nm from 0-4 M Urea concentration. The red line of best fit was generated from fifth-degree polynomial fitting and is intended as a guide to the eye. e LC-MS data, confirming the molecular weight of Symmetrin-1