Proteins can fold during their synthesis by the ribosome through the process of co-translational folding. Such co-translational folding occurs out of equilibrium, meaning that the speed of translation can drastically influence the ability of proteins to fold and function.  Changes to translation speed can prevent folding, increase misfolding, cause aggregate formation, and are implicated as causal factors in cystic fibrosis, hemophilia, and certain cancers. Most protein structure prediction methods do not consider the biological process of translation when making predictions and thus neglect the influence of translation speed. I am working to incorporate aspects of the non-equilibrium nature of protein synthesis into the protein sequence-to-structure prediction method SAINT2. The updated software will hopefully improve predictions and provide a tool capable of predicting the influence of changes to translation speed on proteins.