TDTAC: Time-Dependent Torsion Angle Correlations for Biomolecular Assemblies

A dataset containing torsion angle correlation analyses for a nine-component protein degradation complex. The data was generated by Carolina Escobar Palacio and published on figshare on June 2, 2026. It applies the TDTAC framework to map directional, sequential conformational motions within the dBET70 PROTAC, BRD4, and CRL4A E3 ligase assembly.

Use Cases

• Analyze time-lagged propagation of conformational motions based on the TDTAC framework described.
• Identify ubiquitination-competent states based on coordinated rearrangements linking local torsional dynamics to distal catalytic interfaces.
• Map directional correlation pathways based on the analysis of motions originating at the DDB1–CUL4A region.
• Study the effect of small-molecule degraders on structural rearrangements based on the application to the dBET70 PROTAC complex.

Strengths

• The dataset is derived from a complex of nine distinct biomolecular components, providing a multi-protein system context.
• The analysis framework incorporates explicit time lags, enabling quantitative mapping of directional correlations.
• The dataset is openly available under a CC-BY-4.0 license.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• The data is contained within a 24.3 MB PDF file, which may require extraction to be used computationally.

Provenance

Source

figshare

Collection Method

Analysis generated via the Time-Dependent Torsion Angle Correlation (TDTAC) framework applied to molecular simulation data.

Freshness

Last updated 2026-06-02 22:02:13; freshness should be verified.