earticle

영어

In the past few decades, a novel approach named residue specific incorporation was developed to incorporate non-canonical amino acids into the protein with the help the endogenous translational apparatus. In general, the accuracy of the protein translation is maintained by the fidelity nature of amino acyl tRNA synthetases (AARS). Although, the AARS discriminate the cognate amino acid from the other 19 canonical amino acids, it fails to discriminate the close structural analogs of the cognate amino acid. So, structural insight into the active site of AARS and interaction between the non-canonical amino acid and active site will help to expand the non-canonical amino acid analogs for the residue specific incorporation. So, here we applied an in silico approach to evaluate the polyspecificity nature of Escherichia coli methionyl tRNA synthetases towards the reported methionine analogs