Molecular Dynamics Simulation Results for Septin Protein Membrane Binding

All-atom molecular dynamics simulations examine how amphipathic helix domains from the Cdc12 septin protein interact with lipid bilayers. The dataset, authored by S. Mahsa Mofidi and last updated in April 2026, contains results from simulations of single and paired peptide domains. Findings suggest a cooperative binding mechanism where linked domains induce lipid packing defects on planar membranes.

Use Cases

• Analyzing peptide conformation changes upon membrane association based on simulation trajectories.
• Investigating cooperative binding mechanisms based on the interaction of paired amphipathic helix domains.
• Modeling the induction of lipid packing defects based on simulations of membrane-bound peptide tandems.
• Studying the role of conserved salt bridges in peptide-peptide interactions based on solution-phase simulations.

Strengths

• Data is derived from all-atom molecular dynamics simulations, a high-detail computational method.
• Released under a permissive CC-BY-4.0 license, allowing for broad reuse.
• File size is 5.5 KB, indicating a compact and likely focused dataset.

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• The dataset's small size suggests it contains summary or derived data, not raw simulation trajectories.

Provenance

Source

figshare, author S. Mahsa Mofidi

Collection Method

Generated via all-atom molecular dynamics simulations.

Time Range

null

Freshness

Last updated 2026-04 27 17:42:21; freshness should be verified.

Geography

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