Brief closures of gramicidin A channels in lipid bilayer membranes.
Brief closures, so called flickers, gramicidin A channels were observed for glycerol monooleate/n-decane membranes for cesium chloride and hydrochloric acid solutions. The flickers, similar in nature to the flickers observed for physiological channels, were of the order of 1 ms and the interval between flickers was of the order of 50 ms. The flicker-duration and interval between flickers both decrease with voltage. The field dependence of the flickers is consistent with the hypothesis that the membrane forms a dimple when accomodating a dimer in the membrane and that the monomers, on breaking up, are associated over displacements of the order of 2 nm. For similar measurements for glycerol monoleate/hexadecane membranes only rare occurrences of flickers were observed. It is suggested that the flicker phenomenon is governed by the physical and chemical properties of the membrane and the influence of membrane thickness and interfacial free energy is emphasized.
Ring
A
A
D000473:Alkanes; D005989:Glycerides; D006096:Gramicidin / Q000378:metabolism*; D007473:Ion Channels / Q000378:metabolism*; D007700:Kinetics; D008051:Lipid Bilayers / Q000378:metabolism*; D008954:Models, Biological; D013997:Time Factors
D000473:Alkanes; D005989:Glycerides; D007473:Ion Channels; D008051:Lipid Bilayers; D006096:Gramicidin; C005953:monoolein; C007932:n-hexadecane; C012867:decane