The research group of Dr. Norman Metanis, from the Institute of Chemistry, specializes in organic and bioorganic chemistry and has recently published an article in Chemical Science, in which they describe for the first time a method to access human selenoproteins by total chemical protein synthesis. The human body contains 25 selenoproteins, which contain in their sequence the twenty-first encoded amino acid, selenocysteine. About a dozen of these proteins remain functionally uncharacterized or poorly studied. Challenges in accessing these selenoproteins using traditional recombinant expressions have prevented biological characterization thus far. The Metanis group reported the total chemical syntheses of two human selenoproteins, selenoprotein M (SELM) and selenoprotein W (SELW). The synthesis of the more challenging protein SELM, which is longer, was enabled using recent advances in the field of selenocysteine chemistry that was developed in the lab. This approach allows the preparation of selenoproteins in milligram quantities and in homogenous form, which should open new horizons for future studies to pursue a fuller biological understanding of their role in health and disease, which is currently ongoing in the Metanis group.