Fig. 4
From: Single-molecule sensing of peptides and nucleic acids by engineered aerolysin nanopores
Negatively charged peptide sensing by aerolysin engineered pores. a 3D structure of EYQ3 with its electrostatic potential mapped on the peptide molecular surface. b Raw single-channel recording traces upon EYQ3 addition into the cis chamber of wt, K238A, K238Q, K238N, and K238R mutants, respectively. The final concentration of EYQ3 in the chamber was 2 μM. c Dwell time distribution of EYQ3 translocating through the wt (black), K238A (red), K238Q (orange), K238N (green), and K238R (blue) protein pores under +100 mV voltage. d Comparison between dwell time of EYQ3 (green squares), dwell time of DNA (red triangles), and the diameter at R220 region (black circles) for wt and pore mutants
