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Infographic: Reading Proteins with Nanopores

Adapting DNA nanopore sequencing to peptides allows researchers to identify single amino acid differences.

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Sophie Fessl

Sophie Fessl is a freelance science journalist. She has a PhD in developmental neurobiology from King’s College London and a degree in biology from the University of Oxford.

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In a proof-of-concept study, researchers show that nanopore sequencing techniques can be used to interrogate the sequence of a peptide of interest. First they link the peptide to a stretch of DNA and apply a voltage to feed the conjugated molecule through a nanopore embedded in a thin membrane. A helicase molecule then walks along the DNA strand, effectively pulling the DNA and attached peptide back through the pore. As the peptide passes through, changes in the current across the membrane can be measured, providing clues to the amino acid composition of that stretch of the peptide.





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