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. 2012 Apr 1;6(2):116–123. doi: 10.4161/pri.18665

graphic file with name kprn-06-02-10918665-g001.jpg

Figure 1. (A) Schematic of the α-hemolysin pore embedded in a lipid membrane. Unfolded and simple α-helical or β-sheet forming peptides can readily translocate. (B) Typical current trace of Aβ1−40 recorded for 10 sec. The open pore current is 100 pA and each spike represents an event where a single peptide interacts with the pore. Typically for a peptide, large spikes are due to translocations and short spikes are bumping events.