Tomasz Włodarski

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 characterizes the ribosomal exit tunnel's functional complexity across species using molecular dynamics simulations, revealing dynamic changes and lineage-specific features.

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.

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

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