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Published August 8, 2025 | Version version1
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Study of Protein-Protein Interactions in Septin Assembly: Multiple Amphipathic Helix Domains Cooperate in Binding to the Lipid Membrane

  • 1. Center for Computational Biology, Flatiron Institute, New York, NY
  • 2. Department of Applied Physical Sciences, UNC Chapel Hill, NC
  • 3. Department of Cell Biology, Duke University, Durham, NC
  • 4. Department of Mathematics, UNC Chapel Hill, NC

Description

This repository contains data, analysis scripts, and figures used in the study of amphipathic helix (AH) domains in septin assembly. Using all-atom molecular dynamics simulations, the work explores how single and multiple AH peptides interact with lipid bilayers, including membrane-induced curvature, peptide bending, lipid packing defects, and peptide-peptide interactions. The findings contribute to understanding cooperative membrane binding and septin filament formation.

Files

flatironinstitute/septin_AH_analysis-version1.zip

Files (33.0 MB)

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