Fig. 4

The pairwise hydrophobic surface patch (brown) predictions of 5 cancer-related membrane proteins with their water-soluble QTY variants. For clarity, both extracellular and intracellular regions are removed. The native proteins are on top (A–D). A MGAT3 (top) versus MGAT3^QTY (bottom), B GPR35 (top) versus GPR35^QTY (bottom), C GPR37 (top) versus GPR37^QTY (bottom), D SLC10A1 (top) versus SLC10A1^QTY (bottom), and E NPC1L1 (left) versus NPC1L1^QTY (right). F Global R_H–H_Ƴ distribution of the 1309 QTY designs for all cancer-related membrane proteins in the database. The R_H indicates the content of α-helices in a protein. The hydrophobicity (H_Ƴ) was calculated using the ProPAS and used for evaluating the water solubility of a protein. The T_m index shown in color gradient was calculated using a sequence-based method, which qualitatively represents the stability of a protein. The original membrane proteins are denoted by circles, and the QTY-designed variants are denoted by diamonds. The thin black line shows the corresponding relationship between the original protein and its variant