Type IA Topoisomerase Conformational Dynamics Under Magnesium Modulation

A 397.4 MB multimodal dataset from figshare, published by Yeonee Seol in April 2026, presents findings on how magnesium ions regulate conformational dynamics in Type IA topoisomerases. It integrates data from single-molecule measurements, ensemble experiments, molecular dynamics simulations, and targeted protein mutagenesis. The work reveals a conserved salt-bridge network as a key regulatory mechanism for enzyme function.

Use Cases

• Analyze molecular dynamics simulation trajectories to correlate Mg²⁺ binding with DNA gate opening/closing kinetics.
• Use single-molecule measurement data to model the configurational switching rates of the salt-bridge network.
• Compare ensemble measurement results from wild-type and mutant proteins to validate the role of specific salt-bridge residues.
• Correlate enzyme activity metrics from functional assays with simulated Mg²⁺ concentration levels.

Strengths

• 397.4 MB of integrated data from multiple experimental and computational techniques.
• Findings are based on a combination of single-molecule, ensemble, simulation, and mutagenesis data, providing cross-validation.

Limitations

• Specific row/record counts and individual file structures within the archives are unknown.
• The dataset's primary focus is on a specific enzyme family (Type IA topoisomerases), limiting generalizability.

Provenance

Source

figshare, authored by Yeonee Seol.

Collection Method

Data generated via single-molecule and ensemble measurements, molecular dynamics simulations, and targeted protein mutagenesis.

Freshness

Last updated April 2026.