Published August 8, 2025
| Version version1
Dataset
Open
Study of Protein-Protein Interactions in Septin Assembly: Multiple Amphipathic Helix Domains Cooperate in Binding to the Lipid Membrane
Authors/Creators
- 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)
| Name | Size | Download all |
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md5:c9559bb825a151d0d57705d46f66ebb9
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Additional details
Related works
- Is supplement to
- Software: https://github.com/flatironinstitute/septin_AH_analysis/tree/version1 (URL)
Software
- Repository URL
- https://github.com/flatironinstitute/septin_AH_analysis