Background: Lysine is in the top 3 targets for post-translational modifications (PTMs) within the Uniprot database. Two of these PTMs are carbamylation and glycation, which both non-enzymatically modify lysine with a small molecule. Carbamylation is the modification of a lysine with carbon dioxide and is predicted to affect more than 1.3% of all proteins, with known impacts on human health and protein transcription in plants and mammals. Glycation, the modification of a lysine with a reducing sugar, has various implications in human disease and ageing. However, their full effects are unknown as there are many difficulties in widespread experimental detection. Current computational studies of these modifications have primarily been focused on prediction using only sequence information; however, the accuracy and specificity of these methods suggests that more information is needed. To better understand these modifications, structural information about the modified sites needs to be incorporated. This structural information can be used to characterize modified lysins and predict further modified sites. Furthermore, the effect of these modifications can be studied with molecular dynamic simulations allowing for better understanding of the functional impacts these modifications have on individual proteins. By better characterizing these modifications, the full range of their effects can be understood and mitigated.