John Christodoulou

CryoENsemble improves conformational ensembles from molecular dynamics simulations to better match cryo-EM data and extract dynamics information.

This paper develops NMR methods to measure residual dipolar couplings in the ribosome's dynamic regions, refining structural models and validating them with experimental data.

The paper maps free energy landscapes of an immunoglobulin domain during translation, identifies a kinetic intermediate linked to proline isomerization, and shows the necessity of peptidyl-prolyl isomerases to prevent misfolding.

This paper introduces a new method for analyzing two-dimensional NMR data using quantum mechanical simulations and presents a software tool for this purpose.