DHFR Conformational Dynamics: X-Ray and Simulation Data

Supporting data from a paper describing the conformational dynamics of the enzyme DHFR. The data include several perturbative X-ray diffraction methods and molecular dynamics simulations, authored by Jack B. Greisman. The dataset is hosted on paperswithcode under an Open Access license.

Use Cases

• Analyze protein conformational changes based on perturbative X-ray diffraction data mentioned in the description
• Validate molecular dynamics simulation trajectories based on experimental perturbation data
• Study the effects of ligand, temperature, and electric-field perturbations on enzyme structure

Strengths

• Data originates from a research paper published by an author at Harvard University Press.
• Includes multiple experimental perturbation methods (ligand-, temperature-, and electric-field-based) for cross-validation.

Limitations

• Row count and file 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

Jack B. Greisman, Harvard University Press

Collection Method

Perturbative X-ray diffraction methods and molecular dynamics simulations.