pin-marked" some of them and investigated them with solid-state NMR. Spin-marked proteins contain carbon and nitrogen atoms with an intrinsic magentic moment (spin) which strengthens the NMR's signals. Looking at spectroscopic data before and after the toxin affected the channel, it turned out that the poison attaches to a particular area of the channel ?the pore region ?and changes the area's structure. The poison is thus only effective when it recognises a particular amino acid sequence in the ion channel. It is also important how intrinsically flexible the binding partner is; for a strong interaction to take place, the molecules of both partners have to be able to change their structures.

Applying these new spectroscopic methods, scientists are now better understanding the pharmacology and physiology of potassium channels. This could lead to better, more specific medications.

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Source:Max-Planck-Gesellschaft


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