ArticleFrontiers in molecular biosciences2026
TDTAC: a generalized time-dependent torsion angle correlation framework for resolving directional coordination in large biomolecular assemblies.
Article in Frontiers in molecular biosciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Proteins function through coordinated, time-dependent conformational motions, yet conventional analyses often obscure how these dynamics propagate across complex assemblies. Here, we introduce a generalized Time-Dependent Torsion Angle Correlation (TDTAC) framework that incorporates explicit time lags between residues, enabling quantitative mapping of directional, sequential correlations. By analyzing dihedral rotations, TDTAC reveals conformational dynamics through a physically meaningful representation of residue-level fluctuations. We apply this framework to examine how a small-molecule degrader may induce time-lagged structural rearrangements that facilitate targeted protein degradation. We analyzed the PROteolysis TArgeting Chimera (PROTAC) dBET70, a bifunctional small molecule in complex with its target protein, bromodomain-containing protein 4 (BRD4
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