The human body contains 25 selenoproteins. This is a small family of proteins which contain in their sequence the twenty-first encoded amino acid, selenocysteine. About a dozen of these proteins remain functionally uncharacterized or poorly studied. The bottleneck in studying selenoproteins is the challenges in accessing these proteins using traditional recombinant expressions, which have prevented biological characterization thus far. Chemical protein synthesis has the potential to overcome these hurdles. In a recent seminal paper published in the journal Chemical Science, our group report the first total chemical syntheses of two human selenoproteins, selenoprotein M (SELM) and selenoprotein W (SELW). The synthesis of the more challenging protein SELM was enabled using recent advances in the field of selenocysteine chemistry, which we mastered in our lab. This approach allow 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.