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Fig. 8 | BMC Biochemistry

Fig. 8

From: Identification and characterization of smallest pore-forming protein in the cell wall of pathogenic Corynebacterium urealyticum DSM 7109

Fig. 8

Analysis of the secondary structure of PorACur. a The panel shows the hydrophobicity indices of the individual amino acids of PorACur according to [79]. b The secondary structure of PorACur was predicted using a consensus method at the Pole Bioinformatique Lyonnaise network ( http://npsa-pbil.ibcp.fr/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_seccons.html ) to form α-helices. Amino acid residues were arranged on the basis of heptameric repeats (a-g, rotation of 100 degrees per residue starting from a, in the clockwise direction) showing distinct separation in a hydrophobic domain that could be surrounded by lipid molecules (black) while the hydrophilic domain (grey) is suggested to represent the α-helices orientated to the water-filled lumen of the putative oligomeric PorACur channel

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