Robert B. Best

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.

The paper uses cryo-EM to analyze lambda-6 light chain amyloid structures from different organs and patients, revealing structural diversity and potential interactions with collagen-VI.

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.