Molecular Dynamics Simulations of hGBP1 and hGBP5 Protein Conformations

Bastian F. Bundschuh published a 33.8 MB PDF document on figshare on 2026-05-25. The document presents results from all-atom and coarse-grained molecular dynamics simulations investigating the conformational stability of human guanylate-binding proteins 1 and 5 (hGBP1/5). The study analyzes monomeric and dimeric states with and without GTP bound, focusing on structural transitions relevant to immune function.

Use Cases

• Analyzing protein dimer stability based on stalk interactions and coiled-coil formation described in the study.
• Investigating GTP-induced conformational changes in large GTPases based on simulation results.
• Comparing structural transition mechanisms between hGBP1 and hGBP5 based on the described role of the geranylgeranyl group.

Strengths

• The dataset is a detailed research document (33.8 MB) describing specific molecular dynamics simulation results.
• It focuses on a defined biological system (hGBP1 and hGBP5) with clear relevance to innate immunity.

Limitations

• The primary data format is a PDF (33.8 MB); raw simulation data or structured data tables are not specified.
• Row count and column-level documentation are absent; data extraction would require parsing the document.
• Description metadata is limited; actual data quality requires manual inspection after download.

Provenance

Source

Bastian F. Bundschuh

Collection Method

All-atom and coarse-grained molecular dynamics simulations.

Freshness

Last updated 2026-05-25 08:58:56; freshness should be verified.