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Lulu Enkhbaatar on Muck Rack

Lulu Enkhbaatar

As seen in: BioRxiv
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Articles

The intrinsically disordered C-terminal domain of bacteriophage T4 gp32 amplifies pre-existing conformational heterogeneity at DNA replication junctions

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By Lulu Enkhbaatar, Andrew Marcus, Peter H. von Hippel
| BioRxiv
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.
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Using transition density models to interpret experimental optical spectra of exciton-coupled cyanine (iCy3)2 dimer probes of local DNA conformations at or near functional protein binding sites

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By Dylan Heussman, Lulu Enkhbaatar, Mohammed Sorour, Kurt Kistler
| BioRxiv
Abstract Exciton-coupled chromophore dimers are an emerging class of optical probes for studies of site-specific biomolecular interactions. Applying accurate theoretical models for the electrostatic coupling of a molecular dimer probe is a key step for simulating its optical properties and analyzing spectroscopic data.
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