Structure-based stabilization of insulin as a therapeutic protein assembly via enhanced aromatic–aromatic interactions

Supporting Information

• Stabilization of Insulin as a Therapeutic Protein Assembly via Enhanced Aromatic-Aromatic Interactions - We provide 12 Supplemental Figures and 12 Supplemental Tables as cited in the main text. The information pertains to five aspects: (i) tabulation of ab initio and molecular mechanics calculations; (ii) details of the crystal structure of TrpB26, OrnB29-insulin, corresponding NMR studies, and comparison with WT insulin; (iii) additional control SEC studies; (iv) additional rat studies; and (iv) details regarding the structural properties of insulin as exploited in protein engineering.