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The amiloride-sensitive epithelial sodium channel, ENaC, is a heteromultimeric protein made up of three homologous subunits (alpha, beta and gamma) (1,2). In vitro, assembly and expression of functional active sodium channels in the Xenopus oocyte is stric ...
Aerolysin is a cytolytic toxin which forms channels in the plasma membranes of eucaryotic cells. The protein is secreted by Aeromonas hydrophila as an inactive protoxin. Its stability and water solubility are conferred by its ability to dimerize. Maturatio ...
Allylic PO-ylides generated from dialkyl or diaryl 2-alkenylphosphonates by treatment with a strong base react with aldehydes to afford 1,3-dienes trans-selectively. The newly formed double bond typically exhibits Z/E ratios of 1:99. [on SciFinder (R)] ...
The technique of template synthesis by electrodeposition in the parallel pores of membranes is enhanced with the alternated deposition of different metals. Filled polycarbonate or alumite membranes constitute regular arrays of embedded wires with diameters ...
The coat protein of bacteriophage Pf3 forms discrete and stable ion channels of uniform size in planar bilayers of asolectin. Its primary sequence suggests a channel formed by a bundle of transmembrane helixes. Since the apparent transmembrane region only ...
Colicins A and N are pore-forming bacterial toxins that kill Escherichia coli cells. Their mode of action involves three steps; binding to specific receptors located in the outer membrane, translocation through this membrane and the periplasm, and channel ...
A Ca2+ sensor based on the admittance change of synthetic membranes supported on derivatized silicon electrodes is reported. The ion-sensitive membranes consist of mixed monolayers of phospholipid and the Ca2+-ligand ETH 1001. The electrodes are characteri ...
Insertion of some protein toxins into membranes proceeds through an unfolding step. The unfolding trigger can be the low pH in endosomes, exposure to body temperature, reduction of disulphide bonds or proteolytic cleavage occurring at the membrane surface. ...
The secondary structure of lactose permease (I) of Escherichia coli reconstituted in lipid membranes was detd. by Raman spectroscopy. The a-helix content was .apprx.70%, the b-strand content was
