Ion interactions in (1-13C)D-Val8 and D-Leu14 analogs of gramicidin A, the helix sense of the channel and location of ion binding sites.
Ion-induced chemical shifts in the carbonyl carbon resonances of synthesized ad verified (1-13C)D-Val8 gramicidin A and (1-13C)D-Leu14 gramicidin A are utilized in combination with the previously determined location of the ion binding sites of the gramicidin A channel (using the carbonyls of L-residues) to determine that the helix sense of the gramicidin A channel) is left-handed. Having resolved the handedness issue, the location of the ion binding sites (which are fundamental to understanding the mechanism of ion transport) are further delineated with the results indicating two sites separated by just over 20 A. Furthermore, the demonstration that the divalent barium ion interacts at the binding site while not being transported through the channel is used to argue that the mechanism of monovalent vs. divalent cation selectivity is due to the positive image force contribution to the central barrier.
D001692:Biological Transport; D002247:Carbon Isotopes; D006096:Gramicidin / Q000138:chemical synthesis*; D007473:Ion Channels / Q000502:physiology; D008051:Lipid Bilayers; D008954:Models, Biological; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D002247:Carbon Isotopes; D007473:Ion Channels; D008051:Lipid Bilayers; D006096:Gramicidin