Escherichia colilow molecular mass penicillin-binding pro-teins (PBPs) include PBP4, PBP5, PBP6 and PBP6b. Evi-dence suggests that these proteins interact with the inner membrane via C-terminal amphiphilica-helices. Nonethe-less, the membrane interactive mechanisms utilized by the C-terminal anchors of PBP4 and PBP6b showdifferences to those utilized by PBP5 and PBP6. Here, hydrophobic moment-based analyses have predicted that, in contrast to the PBP4 and PBP6b C-termini, those of PBP5 and PBP6 are candidates to form oblique orientateda-helices
