Formation of large,ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli

One of the major proteins of the outer membrane of Escherichia coli, the matrix protein (porin), has been isolated by detergent solubilisation. When the protein is added in concentrations of the order of 10 ng/cm³ to the outer phases of a planar lipid bilayer membrane, the membrane conductance increases by many orders of magnitude. At lower protein concentrations the conductance increases in a stepwise fashion, the single conductance increment being about 2 nS ($\text{1}\text{nS}\text{= 10}{}^{\mathrm{?9}}\text{siemens}\text{= 10}{}^{\mathrm{?9}}\text{Ω}{}^{\mathrm{?1}}$) in 1 M KCl. The conductance pathway has an ohmic current vs. voltage character and a poor selectivity for chloride and the alkali ions. These findings are consistent with the assumption that the protein forms large aqueous channels in the membrane. From the average value of the single-channel conductance a channel diameter of about 0.9 nm is estimated. This channel size is consistent with the sugar permeability which has been reported for lipid vesicles reconstituted in the presence of the protein.