Benjamin Schuler

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 investigates how linker histone H1.0 binds to nucleosomes and DNA, revealing multiple pathways facilitated by histone chaperones like Nap1.

This paper optimizes force fields for simulating disordered proteins and condensates using osmometry data, improving agreement with experimental measurements.

This study investigates time rescaling in residue-level coarse-grained simulations of complex coacervates, showing that time rescaling factors depend on composition and observable, not just thermodynamic agreement.

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

The paper investigates how sequence variation affects the dynamics of intrinsically disordered proteins, finding that reconfiguration times are largely independent of sequence despite changes in chain dimensions.

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

This study identifies the molecular interactions between lamin isoforms and chromatin, revealing their role in chromatin organization and epigenetic regulation.

The paper investigates the role of stereochemistry in disordered protein-protein interactions, finding that chirality is inconsequential in fully disordered complexes but essential when folding and binding are coupled.