Christopher A. Waudby

This study determines the solution structure and dynamics of MERS-CoV nsp10, revealing intrinsic disorder and identifying potential ligands through NMR fragment screening.

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 identifies peptide ligands that bind i-motif DNA structures and modulate c-Myc gene expression in HEK293 cells.

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

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 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.