John C. Christodoulou

This study investigates the formation of the earliest structure during protein folding on the ribosome and identifies sub-ensembles that may facilitate co-translational folding.

This study structures two co-translational folding intermediates of an immunoglobulin-like domain using NMR and MD simulations, revealing parallel folding pathways conserved within the domain family.

The paper investigates how protein conformational dynamics reveal hidden post-translational modification sites and their functional relevance across timescales.

This study identifies non-native amide-π interactions stabilizing a transient intermediate state in amyloid-forming human lysozyme using NMR and MD simulations.

This paper designs 19F NMR labels to improve chemical shift dispersion and enable structural analysis of proteins and their interactions.

The paper investigates the earliest steps of protein misfolding during alpha-1-antitrypsin biosynthesis, revealing co- and post-translational folding pathways and their implications for disease.

The paper uses structural biology techniques to study how nascent polypeptide chains fold through two distinct pathways during ribosome-mediated translation.

The paper shows that electrostatic repulsion between the ribosome and nascent proteins inhibits co-translational folding, with net charge being the main determinant of folding thermodynamics.

This study identifies small molecules that target the intrinsically disordered ensemble of α-synuclein, showing they can inhibit misfolding, restore phagocytosis, and block cellular transmission of α-synuclein.