Thomas R. Sisk

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.

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.

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.

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