Alkistis N. Mitropoulou

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 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.

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