Paul Robustelli

How small molecules stabilize oligomers of a phase-separating disordered protein

This study investigates how small molecules stabilize oligomers of the androgen receptor activation domain using molecular dynamics simulations and NMR spectroscopy, revealing mechanisms that inform inhibitor design.

Characterizing structural and kinetic ensembles of intrinsically disordered proteins using writhe

This paper uses writhe to analyze conformational ensembles and dynamics of intrinsically disordered proteins, showing it improves Markov state models and enables equivariant neural network sampling.

Determining accurate conformational ensembles ofintrinsically disordered proteins at atomic resolution

This study develops a method to determine accurate atomic resolution conformational ensembles of intrinsically disordered proteins by integrating MD simulations with experimental data using maximum entropy reweighting.

Monomer binding modes of small molecules that modulate the kinetics of hIAPP amyloid formation

This study uses molecular dynamics simulations to investigate how small molecules bind to hIAPP monomers and affect amyloid formation kinetics.

Ensemble docking for intrinsically disordered proteins

This study introduces ensemble docking methods to predict small molecule binding affinities and dynamics for intrinsically disordered proteins, showing agreement with experimental data.

Covalent adducts formed by the androgen receptor transactivation domain and small molecule drugs remain disordered

This study uses molecular dynamics simulations to show that covalent adducts of small molecules with the disordered androgen receptor transactivation domain lead to heterogeneous, collapsed conformations.