Computational Study of Single-Protein Sensing using Nanopores

Identifying the protein content of a cell in fast and reliable manner would represent an important achievement field proteomics. Nanopores, which have been demonstrated to be highly capable sequencing DNA, are now also considered for single-protein studies. Here, we computationally explore potential cylindrical-shaped nanopore created silicon nitride sense distinguish two mini-proteins similar geometry. Sensing could achieved by analyzing magnitude duration modulations ionic current during translocation. We employed molecular mechanics compare occupied pore currents computed based on trajectory ions passing through nanopore. Furthermore, density functional theory was used along with relative surface accessibility values compute changes interaction energies single amino acids obtain dwell times. While remained inside nanopore, found no noticeable differences when subjected 0.5 V 1.0 simulated bias voltages. Dwell times were estimated translocation time that exhibits walls. both feel attractive force wall their differ one order magnitude. This finding implies even cases where proteins virtually indistinguishable current, might still as definite factor reliably identify them.