SuperMyo A339 Protein Mechanical Stability Data from Single-Molecule Experiments

Experimental data from a study on the 'Neighbor Peptide Effect' in the de novo designed protein SuperMyo A339. The dataset likely contains measurements from single-molecule force spectroscopy and steered molecular dynamics simulations, showing how a specific linker peptide enhances mechanical stability. It was authored by Yanwei Wang and last updated on May 4, 2026.

Use Cases

• Training models to predict protein unfolding forces based on sequence and topology features mentioned in the description.
• Analyzing the relationship between linker sequence and mechanical stability enhancement described in the study.
• Validating molecular dynamics simulations of protein unfolding against experimental force spectroscopy data.
• Benchmarking protein design strategies that incorporate interfacial peptide interactions.

Strengths

• Data is derived from controlled single-molecule force spectroscopy experiments, providing direct mechanical measurements.
• Includes specific quantitative results, such as a ~15% stability increase and unfolding forces of ~350 pN and ~400 pN.
• Released under a permissive CC-BY-4.0 license, allowing for broad reuse and modification.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment for large-scale statistical analysis.
• The dataset is very small (43.4 KB), indicating a limited scope likely focused on key experimental results.

Provenance

Source

figshare

Collection Method

Data likely generated from laboratory single-molecule force spectroscopy and computational steered molecular dynamics simulations.

Time Range

null

Freshness

Last updated 2026-05-04 05:30:19; freshness should be verified.

Geography

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