Mourot_2007_ACS.Chem.Biol_2_451

Chemical modification of proteins with bifunctional reagents has become a widely used technique for analyzing protein structure and dynamics. A new era is emerging, and scientists can now actually control the function of proteins by tethering molecular switches at a desired position. In a new paper, researchers stretch the technique a bit further by using a reactive derivative of a peptide toxin to probe the subunit composition of a voltage-gated K+ channel.