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Báo cáo Y học: Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction

Chia sẻ: Nguyen Thang | Ngày: | Loại File: PDF | Số trang:9

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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....

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Nội dung Text: Báo cáo Y học: Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction

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