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Average single-channel conductance, <i>G</i>, of HlyA<sub>Δ71–110</sub> and HlyA<sub>Δ264–286</sub> in different salt solutions.<sup>a.</sup>
Abstract
a<p>The membranes were formed from 1% (mass/volume) asolectin dissolved in n-decane. The aqueous solutions were unbuffered and had a pH of 6. The applied voltage was 20 mV, and the temperature was 20°C. The average single-channel conductance, <i>G</i> (i.e. current divided by voltage), was calculated from at least 80 single events. The standard deviation of the single-channel conductance was generally below ±15%. <i>c</i> is the concentration of the aqueous salt solutions. The single-channel conductance of wildtype HlyA of <i>E. coli</i> is given for comparison <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0112248#pone.0112248-Benz3" target="_blank">[28]</a>. The values denoted with an asterix were measured during this study with purified HlyA. n.m. means not measured.</p><p>Average single-channel conductance, <i>G</i>, of HlyA<sub>Δ71–110</sub> and HlyA<sub>Δ264–286</sub> in different salt solutions.<sup>a.</sup></p- Dataset
- Dataset
- Biological Sciences
- 110 kDa
- Several Amino
- pore formation
- channel structure
- structure predictions
- channel diameters
- acid residues 238
- lipid bilayers
- RTX toxins
- Osmotic protection experiments
- Lipid bilayer measurements
- mutants part
- HlyA transmembrane channel
- wildtype HlyA channels
- wildtype toxin
- 1.8 nm
- HlyA mutants
- wildtype HlyA
- transmembrane pores