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. 2022 Jan 18;204(1):e00214-21. doi: 10.1128/JB.00214-21

FIG 3.

FIG 3

Hydrophobic interactions sequester gp28 in the membrane. (A) The 56-residue phiKT gp28 small protein and the human LL-37 peptide are shown residues with positively (blue) and negatively (red) charged residues highlighted. RaptorX-predicted secondary structure distributions are displayed below. A helical wheel projection of gp28 is displayed with polar faces marked. (B) Whole cell lysate (WCL) from MG1655 (λ900 RzamRz1am) cells with a pRE plasmid encoding the indicated protein were collected 55 min after induction and subjected to repeated ultracentrifugation steps to fractionate supernatant (S/N) from soluble (S) and insoluble pellet (P) proteins. Western blots of gp28 (top), and its control Rz1-His (bottom). Additionally, the pellet fraction was exposed to PBS, 2 M KCl or 6 M urea for solubilization before blotting where indicated.