Mark F. Nüesch

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.

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.