Snapshot showing cholesterol contacts with the N-terminus of p2 and H2 and H3 of p1 in the <i>Surface</i> model.

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• Initial simulation coordinates. A) p7 amino acids and their corresponding position within the protein. B) Two p7 monomers separated (<i>Sep</i> model) and C) extracted from the hexameric structure PDBID 2M6X (initial <i>Bound</i> model configuration). D) Two monomers initially attached by N-termini to the surface of a complex membrane (<i>Surface</i> model) containing DOPC (in green), DPPE (in blue), POPI (in purple), Cholesterol (in black) and DOPS (in orange) (55:21:11:9:4 mol%). Monomers are in the initial positioning seen in replica 1. Water atoms shown with sky blue. Proteins are shown with cartoon representation and differentiated in pink and ice-blue (p1 and p2, respectively); when shown, non-polar residues in white, polar in green and cationic in blue. In snapshots, water and ions are omitted for clarity.
  由: Oluwatoyin Campbell (14392137)
  出版: (2025)
• RMSF per residue in individual p7 monomers for each <i>Sep</i> and <i>Surface</i> model replica.
  由: Oluwatoyin Campbell (14392137)
  出版: (2025)
• Contact maps of residues during the last half of trajectory (200 ns in <i>Sep</i> and 500 ns in <i>Surface</i> model), based on a cutoff of 14 Å.
  由: Oluwatoyin Campbell (14392137)
  出版: (2025)
• Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems.
  由: Oluwatoyin Campbell (14392137)
  出版: (2025)
• Suggested mechanism of p7 dimerization at the ER membrane surface, based on results from this study.
  由: Oluwatoyin Campbell (14392137)
  出版: (2025)