Study of Protein-Protein Interactions in Septin Assembly: Multiple amphipathic helix domains cooperate in binding to the lipid membrane
Fig 2
Bound peptide adopts a stable and smile-like curvature in the membrane.
(A) MD simulation snapshot of a membrane-bound extended AH, with the N-terminus in blue and the C-terminus in red. Arrows indicate hydrophobic residues in the extended regions that face outward toward the solution, unlike the hydrophobic face of the AH region that orients inward. (B) Snapshot of the spatial map of area per lipid (APL) in the membrane upper leaflet. The presence of the peptide increases local APL near its binding site. The dots indicate the position of the backbone alpha carbons. (C) Peptide conformation color-coded by local bending angle using the Bendix tool. (D) Residue-resolved local bending angle (blue, left axis) and corresponding radius of curvature (red dashed, right axis) corresponding to the Bendix snapshot. (E) The local helix bending angle map over simulation time shows stability in the local bending of the membrane-bound peptide. N-terminal residues bend more than those on the C-terminal side.