Abstract

Solid-state nanopores made of silicon nitride have emerged as novel platforms for biosensing such as real-time single-molecule characterization of protein molecules. Solid-state nanopore detection is based on measuring the variations in ionic conductance as charged biomolecules translocate through nanometer-sized channels driven by an external voltage applied across the membrane. In this study, we characterize Avidin (MW: ∼67 kDa) and Case9 (MW: ∼160 kDa) proteins with nanopore current signal. We study how voltage and glycerol, impact on the time durations and current blockage amplitudes produced by the proteins passing through a nanopore.

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