• Protein nanopores: pore-forming proteins are used to create nanoscale holes called nanopores
• Solid-state nanopores: holes created in synthetic materials, such as silicon nitride

The Company's first generation of nanopore sensing systems use a protein nanopore made from the heptameric protein alpha-hemolysin (AHL).  In nature AHL is secreted by bacteria as a tool for forming pores in target membranes.  This offers many advantages in the industrial setting. It is easily and cheaply produced using bacteria, it can be modified with angstrom-level precision using biochemical or molecular biological techniques, and the protein is very robust.
AHL has been characterised and studied at great length by the founder Professor Hagan Bayley, other Company collaborators, and extensively within the Company.  It can be adapted with a variety of adapter molecules for the analysis of DNA, proteins and other target analytes.    
In exonuclease sequencing, individual DNA bases cleaved from a strand are identified by the nanopore.  The nanopore is adapted with a cyclodextrin molecule to create a binding event as bases pass through the pore, thus enabling high accuracy base identification.  The nanopore is also coupled with a processive enzyme.
The strand sequencing method requires the identification of individual bases on a single strand as it passes through the nanopore. Oxford Nanopore is developing this method in house through internal R&D and collaboration with leading academic experts in nanopore sensing.  The nanopore is engineered to discriminate the identity of a single DNA base among many on a strand, and this nanopore is again coupled with a processive enzyme to control translocation of the DNA through the pore.
Nanopores can also be adapted for the analysis of proteins in solution.  By attaching a ligand to a nanopore that has been designed to bind specifically with a target protein, it is possible to detect the presence of that protein electronically. When the protein binds with the ligand, the current disruption can be measured.  This method provides richer information about the molecular interaction; the duration and frequency of binding events can be recorded, allowing further analyses on the analyte concentration and other characteristics. 
Other modifications can be made for the analysis of small molecules.

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