ArticlebioRxiv : the preprint server for biology2026
The intrinsically disordered C-terminal domain of bacteriophage T4 gp32 amplifies pre-existing conformational heterogeneity at DNA replication junctions.
Article in bioRxiv : the preprint server for biology, 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
Selective molecular recognition of dynamic nucleic acid structures is fundamental to DNA replication, yet the physical mechanisms by which intrinsically disordered protein domains achieve this selectivity remain poorly understood. Here, we investigate how the intrinsically disordered C-terminal domain (CTD) of the bacteriophage T4 single-stranded DNA-binding protein gp32 contributes to the recognition of ss-dsDNA replication fork junctions. Using absorbance, circular dichroism, and two-dimensional fluorescence spectroscopy (2DFS) of model DNA replication junctions containing an exciton-coupled (Cy3)
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