Figure 3: Hydrophobic and charge patterns associated with GyrA amino acid substitutions.

From: Development and characterisation of highly antibiotic resistant Bartonella bacilliformis mutants

Figure 3: Hydrophobic and charge patterns associated with GyrA amino acid substitutions.
Figure 3

(A) Alterations in the hydrophobic pattern. Additionally to the amino acid substitutions detected (Ala-91 → Val and Asp-95 → Gly) the theoretical effect of the presence of Ser-91 also shows the gradual effect on the hydrophobic pattern related to the presence of Ser, Ala or Val at position 91. (B) Effect on the charge pattern. This graph only shows the effect of Asp-95 and Gly-95 since the presence of Val-91 does not result in charge pattern alterations. The (A) comprises the amino acid sequence from amino acids 84 to 99, while in (B) the amino acid sequences analysed are from amino acids 70 to 107.