Key result
A reactive derivative of a peptide toxin was used as a bifunctional reagent to probe the subunit composition of a voltage-gated K+ channel.
Chemical modification with bifunctional reagents allows for the probing of subunit composition and control of protein function in voltage-gated K+ channels.
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.
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Mourot et al. (2007) reported an editorial. Reactive derivative of a peptide toxin was evaluated. A reactive derivative of a peptide toxin was used as a bifunctional reagent to probe the subunit composition of a voltage-gated K+ channel.
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