Single-Molecule Force Spectroscopy of Prion Protein and Pentosan Polysulfate

Force extension curves showing unfolding and refolding transitions measured for hamster prion protein (PrP) in the presence of pentosan polysulfate (PPS). The data consist of extension (nm) and force (pN) values from successive individual unfolding and refolding trajectories. The dataset was contributed by R. A. Petrosyan and is available via paperswithcode under an Open Access license.

Use Cases

• Analyze protein unfolding and refolding kinetics based on force-extension trajectories.
• Model the mechanical stability of prion proteins based on force spectroscopy measurements.
• Investigate the effect of the ligand pentosan polysulfate on protein folding pathways based on the described interaction data.

Strengths

• Data contains specific physical measurements of extension in nanometers and force in piconewtons.
• The description indicates data is organized by individual molecule pulling/relaxation curves in separate sheets.

Limitations

• Row count and total dataset size are unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

R. A. Petrosyan via paperswithcode

Collection Method

Single-molecule force spectroscopy measurements.