Lisa D. Cabrita

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.

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.