Peter H. von Hippel

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.