Norman Metanis

1 INTRODUCTION Chiral control over translation is a prerequisite for reliably encoding well-defined protein conformations. Although both homochiral and heterochiral peptides can adopt complex, stable structures (Urry et al. 1971; Veatch et al. 1974), this is almost always achieved in the context of a defined pattern of amino acid chirality. The incorporation of even a single mirror-image amino acid into a contemporary protein can be significantly destabilizing (Krause et al.

Natural protein folding takes place in aqueous cell environments. Now, it has been found that proteins in a water-free environment undergo faster and more efficient folding.

The semisynthesis of nucleolar human selenoprotein H The human selenoprotein H is the only selenocysteine-containing protein that is located in the cell’s nucleolus. In vivo studies have suggested that it plays some role in DNA binding, consumption of reactive oxygen species, and may serve as a safeguard against cancers. However, the protein has never been isolated and, as a result, not yet fully characterized.