Abstract:Abstract. The paramagnetism of a lanthanoid tag site-specifically installed on a protein provides a rich source of structural information accessible by nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy. Here we report a lanthanoid tag that reacts selectively with cysteine or selenocysteine with formation of a (seleno)thioether bond and a short tether between lanthanoid ion and protein backbone. The tag is assembled on the protein in three steps, comprising (i) reaction wit… Show more
Stapling of peptides renders them ideal drug candidates. We report a new peptide staple resembling the natural metabolite lanthionine ketenamine. The strategy is orthogonal to canonical amino acids, proceeds in...
Stapling of peptides renders them ideal drug candidates. We report a new peptide staple resembling the natural metabolite lanthionine ketenamine. The strategy is orthogonal to canonical amino acids, proceeds in...
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