Daniel Nettels

This study quantifies how phosphorylation modulates electrostatic interactions between charged IDPs and RNA, showing that phosphorylation reduces binding affinity linearly with net charge.

This study examines how charge patterning affects the conformational behavior and dynamics of intrinsically disordered proteins using experimental techniques and simulations.

This study uses time-resolved single-molecule FRET to show that PAR length determines nucleosome decompaction efficiency and reversibility.

The paper introduces a model-free method to analyze diffusion-based single-molecule FRET experiments, showing it accurately captures protein dynamics without artifacts from photon trajectory length or diffusion.