Anaïs M. E. Cassaignau

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 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.