title: On the mechanism of channel-length dependence of gramicidin single-channel conductance.
abstract: Single-channel conductance data on four different gramicidin channel lengths demonstrate that conductance magnitude is neither inversely dependent on the square of the channel length nor on the image force arising from differences in the extent of lipid dimpling (Jordan and Vayl (1985) Biochim. Biophys. Acta 818, 416-420). Rather the conductance differences are consistent with the decreased off-rate constant for the singly occupied state as the ionic radius decreases from that of cesium ion to sodium ion coupled with the decreased probability of the doubly occupied channel due to increased ion-ion repulsion as the channel is shortened (Urry et al. (1984) Biochim. Biophys. Acta 774, 115-119).
mesh_terms: D002586:Cesium / Q000378:metabolism; D004553:Electric Conductivity; D006096:Gramicidin / Q000378:metabolism* / Q000031:analogs & derivatives; D007473:Ion Channels / Q000502:physiology*; D008051:Lipid Bilayers / Q000378:metabolism; D008081:Liposomes / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D011188:Potassium / Q000378:metabolism; D012964:Sodium / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D007473:Ion Channels; D008051:Lipid Bilayers; D008081:Liposomes; C040526:gramicidin A, 7,8-des-Val-; D006096:Gramicidin; D002586:Cesium; D012964:Sodium; D011188:Potassium