Supplementary Fig. 12: Discrimination of LR7 and IR7 under optimized recording conditions.
From: Electrical recognition of the twenty proteinogenic amino acids using an aerolysin nanopore

Histograms of relative residual current Ib/I0 measured using a low-noise setup (see Supplementary Note 3). The nanopore experiments were performed using an equimolar mixture of LR7 and IR7 peptides and under the following experimental conditions: –50 mV in 4M KCl (a, n = 3474 events); –40 mV in 4M KCl (b, n = 2373 events); –40 mV in 2M KCl/2M KNO3 mixture (c, n = 3437 events). In 4M KCl, the diminution of the voltage magnitude from –50 mV to –40 mV leads to a reduction of the standard deviations of the two main populations, and a shift of the Ib/I0 values from 0.380 ± 0.0018 to 0.378 ± 0.0013 (LR7) and from 0.384 ± 0.0016 to 0.382 ± 0.0012 (IR7). At –40 mV, the substitution of 50% of the Cl– ions by 50% of NO3– ions further reduces the standard deviations of the two main populations now located at Ib/I0 values of 0.382 ± 0.0010 (LR7) and 0.386 ± 0.0010 (IR7). Continuous lines show the underlying Gaussian distributions. The mean value (respectively uncertainty) of relative residual current of each peptide was obtained as the mean value (respectively standard deviation) of a gaussian fit of the corresponding Ib/I0 distribution; from single independent experiments. The data were acquired at room temperature and under a voltage bias applied to the trans compartment.