Conformational analysis of arginine methylated and di methylated and serine phosphorylated in silico

post-translational modifications (PTMs) encompass alterations to the side chains of amino acids subsequent to their synthesis. These modifications play pivotal roles in regulating diverse cellular processes, such as kinase activation, protein degradation, and more. Additionally, they exert a significant influence on the functionality and architecture of the proteins within which these processes occur. Depending on the specific amino acid affected and its location, these modifications can contribute to the development of various diseases. Through Density Functional Theory (DFT) calculations, we delve into the structural ramifications of PTMs on amino acids, exploring whether they might contribute to their deregulation. We recognize that these modifications do indeed alter the orientation of amino acids, which may play a significant role in the development of various diseases or even their initiation. Additionally, we observe PTMs also have an impact on several characteristics of amino acids, such as dipolar moment, highest occupied molecular orbital (HOMO), lowest unoccupied molecular orbital (LUMO), and partial charge. This suggests that modifying these features can potentially influence factors like the stability of the amino acid or even the entire protein. Through this study, we can conclude that by adopting this approach, we can gain deeper insights into the influence of PTMs on amino acids and whether such influences can be directly linked to the development of diseases associated with PTM deregulation.