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. 2018 Aug 31;7:e40889. doi: 10.7554/eLife.40889

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© 2018, Entova et al

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Figure 3. — (A) Dynamic hydrogen bonding between the side chain hydroxyl (top panel) or backbone amide-NH (bottom panel) of Ser23 and the backbone amide-C=O of Leu19 and Ile20 measured during MD simulations of PglC in a POPE lipid bilayer. (B) Peptides corresponding to the RMH domains of wild-type (top) and S23A/P24A PglC (bottom) were folded from an extended conformation (left panel) for 100 ns in water (middle panel), followed by an additional 1500 ns in 20% isopropanol/water (right panel).

Figure 3—figure supplement 1. — (A) Dynamic hydrogen bonding between the side chain hydroxyl (top panel) or backbone amide-NH (bottom panel) of Ser23 and the backbone amide-C=O of Leu19 and Ile20 measured during MD simulations of PglC in a POPE lipid bilayer. (B) Peptides corresponding to the RMH domains of wild-type (top) and S23A/P24A PglC (bottom) were folded from an extended conformation (left panel) for 100 ns in water (middle panel), followed by an additional 1500 ns in 20% isopropanol/water (right panel).