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Beta-barrel pores are found in outer membrane porins of Gram-negative bacteria, bacterial toxins and mitochondrial channels. Apart from the β-barrel the three groups show no close sequence or structural homology but these pores exhibit symmetrical voltage gating when reconstituted into planar lipid bilayers. The structures of several of these are known and many site-directed mutants have been examined...
Three sulfhydryl labels were used to modify two mutated sites, R37C and R74C in the eyelet of the outer membrane porin OmpC. Modification of R37C with the neutral groups Aldrithiol and bimane increases thermal stability but the negatively charged iodoacetate causes a decrease in thermal stability. The effects of substitution at R74C were less significant. Bimane labelling increases the voltage sensitivity...
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