Variable ion channels: A 22mer peptide derived from the D,L-peptide gramicidin A changes from an inactive to a highly ion-channel-active conformation (see picture). The helical structure of the active and inactive conformations was characterized by NMR spectroscopy and circular dichroism; conductance measurements led to the conclusion that there are two symmetrical binding sites for the Cs atom in the active form.
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Arndt et al. (2002) studied this question.