Andrew H. Marcus

This study shows that the intrinsically disordered C-terminal domain of gp32 amplifies conformational heterogeneity in DNA replication junctions, enhancing selective recognition without stabilizing a single conformation.

This study investigates how gp32 coordinates DNA replication in bacteriophage T4 by analyzing its interactions with ssDNA and ss-dsDNA junctions using single-molecule techniques.

The paper analyzes single-molecule fluorescence data to quantify free energy surfaces of DNA breathing at replication fork junctions.

This paper introduces 2PE-2DFS to study DNA base conformations using 6-MI, revealing electronic-vibrational spectra and conformation-dependent exciton coupling in dimers.

This paper introduces a single-molecule fluorescence method to measure DNA breathing dynamics using (iCy3)2 dimer probes, revealing four conformational macrostates in DNA fork constructs.

The paper uses transition density models to analyze optical spectra of (iCy3)2 dimer probes, determining DNA conformational parameters near protein binding sites.